Information on EC 3.2.1.17 - lysozyme:
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EC NUMBERCOMMENTARY
3.2.1.17-

RECOMMENDED NAMEGeneOntology No.
lysozymeGO:0003796

REACTIONREACTION DIAGRAMCOMMENTARYORGANISM UNIPROT ACCESSION NO.LITERATURE
Hydrolysis of (1->4)-beta-linkages between N-acetylmuramic acid and N-acetyl-D-glucosamine residues in a peptidoglycan and between N-acetyl-D-glucosamine residues in chitodextrins
show the reaction diagram		----
Hydrolysis of (1->4)-beta-linkages between N-acetylmuramic acid and N-acetyl-D-glucosamine residues in a peptidoglycan and between N-acetyl-D-glucosamine residues in chitodextrins
show the reaction diagram		crystallization data and molecular dynamics simulations indicate that lysozyme is an inverting enzyme, and Asp97 acts as a second carboxylate and that the narrow space of the binding cleft at subsites E–G in GEL may prohibit the sugar chain to bind alternative site that might be essential for transglycosylationAnser anser-698655

REACTION TYPEORGANISM UNIPROT ACCESSION NO.COMMENTARYLITERATURE
hydrolysisGadus morhua-cleaving the beta-1,4 glycosidic bond between N-acetyl-D-glucosamine (NAG) and N-acetylmuramic acid (NAM) in the peptidoglycan layer708057
hydrolysisAnopheles gambiaeQ17005hydrolyze the beta-1,4-glycosidic linkage between N-acetylmuramic acid and N-acetylglucosamine of peptidoglycan708225
hydrolysisGallus gallus-lysozyme has a potent antimicrobial effect due to the hydrolysis of the beta-linkage between muramic acid and N-acetyl glucosamine present in the microbial walls708362
hydrolysisApostichopus japonicus-catalyzes the hydrolysis of bacterial cell walls709183
hydrolysisFenneropenaeus merguiensis-lysozyme kills bacteria by hydrolyzing beta-1,4-glycosidic linkages between N-acetylglucosamine and N-acetylmuramic acid of the peptidoglycan layer in the bacterial cell wall709875
hydrolysisEquus caballus-lysozyme hydrolyses 1,4-beta-linkages between N-acetylmuramic acid and N-acetyl-D-glucosamine residues in a peptidoglycan710467
hydrolysis of O-glycosyl bond----
hyrolysis of O-glycosyl bondPseudomonas phage phiKZQ8SD18-683684

PATHWAYKEGG LinkMetaCyc Link
No entries in this field

SYSTEMATIC NAMEIUBMB Comments
peptidoglycan N-acetylmuramoylhydrolasecf. also EC 3.2.1.14 chitinase.

SYNONYMSORGANISM UNIPROT ACCESSION NO.COMMENTARYLITERATURE
1,4-beta-N-acetylmuramidase----
1,4-beta-N-acetylmuramidase 1Musca domestica--681655
1,4-beta-N-acetylmuramidase A/C----
1,4-beta-N-acetylmuramidase M1----
1,4-beta-N-acetylmuramoylhydrolase----
1,4-N-acetylmuramidase----
AcmBLactococcus lactisQ8KKF9-656731
ASTLAmyda cartilaginea--679342
Autolysin----
BA-lysozymeBufo andrewsi--664671
c-type lysozymeAnopheles stephensi--680112
CFLBrassica oleracea--680229
CP-1 lysin----
CP-7 lysin----
CP-9 lysin----
CPL----
Endolysin----
EndolysinStreptococcus phage B30--677671
EndolysinLactobacillus phage phigaY--680003
EQLEquus caballus--682754
equine lysozymeEquus caballus--710467
fOg44 endolysinOenococcus phage fOg44--680524
g-lysozymeLarimichthys crocea--677863
g-type lysozymeSalmo salar--679139
g-type lysozymeGadus morhua--708057
g-type lysozymeHomo sapiensQ86SG7-718120
GEWLAnser sp.--680229
globulin G----
globulin G1----
goose type lysozymeStruthio camelus--680548
Goose-type lysozyme----
Goose-type lysozymeLarimichthys crocea--677863
Goose-type lysozymeSalmo salar--679139, 717510
Goose-type lysozymeChlamys farreriQ075V3-681964
Goose-type lysozymeHomo sapiensQ86SG7-718120
gp144Pseudomonas phage phiKZQ8SD18-683684
gp36CEnterobacteria phage phiKMV--664563
GSTLChelonia mydas--679342
HEWLGallus gallus--677858, 680229, 680380
HLysG2Homo sapiensQ86SG7-718120
HLZHomo sapiens--718276
i-type lysozymeApostichopus japonicus--709183
L-7001----
LALEnterobacteria phage lambda--680229
Late protein gp15----
Lys-rich lysozyme 2Musca domesticaQ7YT17-677356
LYSC-1Anopheles gambiaeQ17005-708225
LysgaYLactobacillus phage phigaY--680003
LysGLLarimichthys crocea--677863
Lysis protein----
Lysosyme----
lysozymGallus gallus--709764
Lysozyme----
LysozymeGallus gallus--707414, 707830, 708358, 708362, 708795, 708875, 709169, 710026, 710491
LysozymeBacillus anthracis--708007
LysozymeRuditapes philippinarum--708061, 708229
LysozymeFenneropenaeus merguiensis--709875
lysozyme 1Musca domestica-precursor681655
lysozyme 1 precursorMusca domesticaQ7YT17-677356
lysozyme cMusca domestica--681655
lysozyme c-1Anopheles gambiaeQ17005-708225
lysozyme g----
lysozyme g-like 2Homo sapiensQ86SG7-718120
lysozyme SP0987Streptococcus pneumoniae--706988
M1LStreptomyces globisporus--680229
Mdl1Musca domestica--681655, 717509
MdL2Musca domestica--717509
mucopeptide glucohydrolase----
mucopeptide N-acetylmuramic acid hydrolaseGallus gallus--718309
mucopeptide N-acetylmuramoylhydrolase----
muramidase----
muramidaseGadus morhua--708057
muramidaseRuditapes philippinarum--708229
muramidaseApostichopus japonicus--709183
muramidaseHomo sapiens--718276
mutanolysinStreptomyces globisporus--680229
MV1 lysin----
N,O-diacetylmuramidase----
N-acetylglucosaminidase autolysinLactococcus lactisQ8KKF9-656731
OELStruthio camelus--680548
Outer wedge of baseplate protein----
P13----
Peptidoglycan hydrolase----
phiKZ endolysinPseudomonas phage phiKZQ8SD18-683684
Ply3626Clostridium phage phi3626-endolysin of bacteriophage phi3626654265
PR1-lysozyme----
Protein gp17----
Protein gp19----
Protein Gp25----
Protein Gp5----
Protein gp54----
Protein gpK----
SalGSalmo salar--679139, 717510
SjLysApostichopus japonicus--709183
SSTL APelodiscus sinensis--679342
SSTL BPelodiscus sinensis--679342
T4 lysozymeEnterobacteria phage T4--718395
TJLRuditapes philippinarum--680812
transglycosylasePseudomonas phage phiKZQ8SD18-683684
VpLYZRuditapes philippinarum-invertebrate type lysozyme708229

CAS REGISTRY NUMBERCOMMENTARY
9001-63-2-

ORGANISMCOMMENTARYLITERATURESEQUENCE CODESEQUENCE DB SOURCE
Amyda cartilaginea-679342--Manually annotated by BRENDA team
Anas platyrhynchos-171083--Manually annotated by BRENDA team
Anas platyrhynchosKaki and wild-type; multiple forms; Peking-duck171076--Manually annotated by BRENDA team
Anas platyrhynchosPeking-duck171050--Manually annotated by BRENDA team
Anopheles gambiae-708225Q17005UniprotManually annotated by BRENDA team
Anopheles gambiaeisoform Lys i-1698287Q7QHB9UniProtManually annotated by BRENDA team
Anopheles gambiaeisoform Lys i-2698287A4ZWD2UniProtManually annotated by BRENDA team
Anopheles stephensi-680112--Manually annotated by BRENDA team
Anser anser-698655, 699629P00718UniProtManually annotated by BRENDA team
Anser sp.-664365, 664786, 665003, 680229--Manually annotated by BRENDA team
Anser sp.goose171084--Manually annotated by BRENDA team
Apostichopus japonicus-709183--Manually annotated by BRENDA team
Bacillus anthracis-708007--Manually annotated by BRENDA team
Bacillus sp.-677778, 679957--Manually annotated by BRENDA team
Bos taurus-171049, 171071, 679303--Manually annotated by BRENDA team
Bos taurus-171093P80189UniprotManually annotated by BRENDA team
Bos taurus-697903Q06283UniprotManually annotated by BRENDA team
Bos taurus4 isoforms171104--Manually annotated by BRENDA team
Bos taurusgastric mucosa: 3 lysozymes c, other tissues: no lysozyme c, low levels of another lysozyme, g class171045--Manually annotated by BRENDA team
Brassica oleraceavar. botrytis664786, 665003, 680229--Manually annotated by BRENDA team
Brassica sp.turnip171069, 171079--Manually annotated by BRENDA team
Bufo andrewsi-664671--Manually annotated by BRENDA team
Canis lupus familiaris-171071, 171098, 678277, 701125--Manually annotated by BRENDA team
Carica papaya-171080--Manually annotated by BRENDA team
Casuarius casuarius-664365--Manually annotated by BRENDA team
Ceratitis capitatadipterous171065--Manually annotated by BRENDA team
Cervidae-171045--Manually annotated by BRENDA team
Chelonia mydas-679342, 682698--Manually annotated by BRENDA team
Chlamys farreri-681964Q075V3SwissProtManually annotated by BRENDA team
Clostridium acetobutylicumATCC 824171101--Manually annotated by BRENDA team
Clostridium phage phi3626murein hydrolase, endolysin Ply3626 of dual lysis system consisting of holin and endolysin654265--Manually annotated by BRENDA team
Colitis bacteriophage-171090--Manually annotated by BRENDA team
Crassostrea virginica-664651--Manually annotated by BRENDA team
Enterobacteria phage K11-680582--Manually annotated by BRENDA team
Enterobacteria phage lambda-665003--Manually annotated by BRENDA team
Enterobacteria phage lambdaexpressed from Escherichia coli TG-1 carrying plasmid pHDM10680229--Manually annotated by BRENDA team
Enterobacteria phage lambdasynthesized in Escherichia coli171087--Manually annotated by BRENDA team
Enterobacteria phage P22enzyme induced in Salmonella typhimurium171077--Manually annotated by BRENDA team
Enterobacteria phage phiKMV-664563--Manually annotated by BRENDA team
Enterobacteria phage T4-171033, 171037, 171042, 171048, 171053, 171070, 171073, 664786, 665003, 680229, 718395--Manually annotated by BRENDA team
Enterobacteria phage T4-682730, 696225, 700964P00720UniprotManually annotated by BRENDA team
Enterobacteria phage T4enzyme is product of e gene for lysis from within, or gene 5 for lysis from without171052--Manually annotated by BRENDA team
Enterobacteria phage T4wild-type and mutant171060--Manually annotated by BRENDA team
Enterobacteria phage T7-680582--Manually annotated by BRENDA team
Equus caballus-171091, 682754, 710467, 718376--Manually annotated by BRENDA team
Equus caballusexpression of recombinant Ca2+-binding lysozyme in Aspergillus niger171109--Manually annotated by BRENDA team
Equus caballusmare171074--Manually annotated by BRENDA team
Escherichia coliphage T4 induced171042, 171048--Manually annotated by BRENDA team
Fenneropenaeus merguiensis-709875--Manually annotated by BRENDA team
Ficus sp.-171086--Manually annotated by BRENDA team
Gadus morhua-708057--Manually annotated by BRENDA team
Galleria mellonella-698030--Manually annotated by BRENDA team
Gallus gallus-171039, 171043, 171044, 171056, 171057, 171062, 171063, 171068, 171069, 171089, 171092, 171094, 171099, 171105, 171106, 171107, 663508, 663510, 663529, 664351, 664368, 664786, 665003, 665993, 666541, 666704, 677858, 678407, 678484, 679189, 679544, 680207, 680229, 680255, 680380, 680954, 681060, 681598, 681709, 682603, 707414, 707830, 708358, 708362, 708795, 709169, 709764, 710026, 710491, 717036, 717301, 717672, 718309, 718362--Manually annotated by BRENDA team
Gallus gallus-663498, 665757, 678844, 680541, 683018, 695524, 696021, 696408, 696414, 696471, 696840, 698409, 698462, 698654, 699048, 699054, 699629, 699858, 700151, 700911, 701132, 708875P00698UniProtManually annotated by BRENDA team
Gallus gallus101-succinimide lysozyme171035--Manually annotated by BRENDA team
Gallus gallusexpression of recombinant Ca2+-binding lysozyme in Aspergillus niger171109--Manually annotated by BRENDA team
Gallus gallushuman cell lines HeLa and MCF-7171038--Manually annotated by BRENDA team
Gallus gallustwo domains crosslinked between Trp62 and Asp101171103--Manually annotated by BRENDA team
Gallus galluswild-type and engineered enzyme expressed in Saccharomyces cerevisiae171111--Manually annotated by BRENDA team
Helicoverpa armigera-695906Q19R28UniProtManually annotated by BRENDA team
Helicoverpa zea-665818--Manually annotated by BRENDA team
Heliothis virescens-171046--Manually annotated by BRENDA team
Homo sapiens-171047, 171066, 171068, 171069, 171075, 171084, 171085, 171088, 171100, 171110, 677858, 677972, 679303, 681099, 682197, 696869, 697428, 699576, 699710, 718273, 718276--Manually annotated by BRENDA team
Homo sapiens-695659P61626UniProtManually annotated by BRENDA team
Homo sapiens-718120Q86SG7UniProtManually annotated by BRENDA team
Homo sapiensexpression of recombinant Ca2+-binding lysozyme in Aspergillus niger171109--Manually annotated by BRENDA team
Homo sapiensgene expression in: Saccharomyces cerevisiae171034, 171036--Manually annotated by BRENDA team
Lactobacillus phage phigaY-680003--Manually annotated by BRENDA team
Lactococcus lactissubsp. cremoris, strain MG1363656731Q8KKF9SwissProtManually annotated by BRENDA team
Larimichthys crocea-677863--Manually annotated by BRENDA team
Liolophura japonica-679934--Manually annotated by BRENDA team
Lysobacter sp.strain XL 1678508--Manually annotated by BRENDA team
Lysobacter sp. XL 1strain XL 1678508--Manually annotated by BRENDA team
Medicago sativa2 forms CHIT24 and CHIT3171096--Manually annotated by BRENDA team
Meleagris gallopavoturkey171069, 171082--Manually annotated by BRENDA team
Micrococcus luteus-679934--Manually annotated by BRENDA team
Mus musculus-717466--Manually annotated by BRENDA team
Musca domestica-677356, 681655Q7YT16SwissProtManually annotated by BRENDA team
Musca domestica-699304B3GQR5UniProtManually annotated by BRENDA team
Musca domesticadigestive lysozymes 1 and 2, i.e. MdL1 and MdL2717509--Manually annotated by BRENDA team
Musca domesticahouse fly171102--Manually annotated by BRENDA team
Musca domesticaLys-rich lysozyme 2 fragment677356Q7YT17SwissProtManually annotated by BRENDA team
Nephtys hombergiiannelid171072--Manually annotated by BRENDA team
Nilssonia gangeticaCuvier tortoise171061--Manually annotated by BRENDA team
Oenococcus phage fOg44-680524--Manually annotated by BRENDA team
Omphalius pfeifferi-679934--Manually annotated by BRENDA team
Oncorhynchus mykisstrout, c-type171041--Manually annotated by BRENDA team
Ornithodoros moubatasoft tick171097--Manually annotated by BRENDA team
Oryctolagus cuniculus-171055, 171108--Manually annotated by BRENDA team
Ovis aries-171045--Manually annotated by BRENDA team
Ovis aries-171093P80190UniprotManually annotated by BRENDA team
Papio cynocephalusbaboon171078--Manually annotated by BRENDA team
Pelodiscus sinensis-679342--Manually annotated by BRENDA team
Pelodiscus sinensis-698657Q7LZQ1UniprotManually annotated by BRENDA team
Penaeus monodon-700107Q8IT75UniProtManually annotated by BRENDA team
Pseudomonas aeruginosaK-187, two extracellular forms FI and FII171095--Manually annotated by BRENDA team
Pseudomonas aeruginosapyocinogenic171058--Manually annotated by BRENDA team
Pseudomonas phage phiKZPseudomonas bacteriophage683684Q8SD18UniProtManually annotated by BRENDA team
Rattus norvegicus-171054, 171064, 171067--Manually annotated by BRENDA team
Rhea americana-664365--Manually annotated by BRENDA team
Rhodnius prolixus-699392A9LN31, A9LN32UniProtManually annotated by BRENDA team
Ruditapes philippinarum-680812, 708061, 708229--Manually annotated by BRENDA team
Ruminantiatype c171045--Manually annotated by BRENDA team
Saccharopolyspora erythraea-171059--Manually annotated by BRENDA team
Salmo salar-679139, 699629--Manually annotated by BRENDA team
Salmo salar-717510A6PZ97UniProtManually annotated by BRENDA team
Saxidomus purpuratus-679932--Manually annotated by BRENDA team
Staphylococcus aureus-171081--Manually annotated by BRENDA team
Streptococcus phage B30-677671--Manually annotated by BRENDA team
Streptococcus pneumoniae-171051, 698818, 706988--Manually annotated by BRENDA team
Streptomyces globisporus-171069, 665003, 680229--Manually annotated by BRENDA team
Struthio camelus-664365, 680548--Manually annotated by BRENDA team
Struthio camelusostrich697868--Manually annotated by BRENDA team
Triticum aestivumwheat, multiple electrophoretic forms171040--Manually annotated by BRENDA team
unidentified phagephiIN93696020Q859R8UniProtManually annotated by BRENDA team
unidentified phageT2, N20F, lambda, F1,F5, Kp, 2, Pf15, A-22, F12,13,14, P1,P14, N1 and others171073--Manually annotated by BRENDA team
unidentified phage phiIN93phiIN93696020Q859R8UniProtManually annotated by BRENDA team
Xanthomonas phage Xop411bacteriophage of Xanthomonas oryzae pv. oryzae682650A1BPG9SwissProtManually annotated by BRENDA team

GENERAL INFORMATIONORGANISM UNIPROT ACCESSION NO.COMMENTARYLITERATURE
physiological functionGallus gallus-influence of the chemical chaperones 4-hexylresorcinol, and 5-methylresorcinol on the structure, equilibrium fluctuations, and functional activity of the hydrophilic enzyme lysozyme, molecular dynamics, overview717301
physiological functionMus musculus-lysozyme activates Enterococcus faecium to induce necrotic cell death in macrophages in vitro and in vivo. Pretreatment of Enterococcus faecium with lysozyme and subsequently with broad spectrum protease considerably reduces cell death, suggesting that a bacterial surface protein is causative for cell death induction.717466
physiological functionHomo sapiensQ86SG7lysozyme plays an important role in human innate immunity by causing bacterial cell lysis. Recombinant HlysG2 inhibits Gram-positive bacterial growth, but does not inhibit Gram-negative bacterial and Candida albicans growth. HLysG2 is a potent antibacterial protein that may play a role in the innate immunity of the human eye718120
physiological functionHomo sapiens-human lysozyme is a key component of the innate immune system. But the wild type protein fails to participate effectively in clearance of certain infections due to inherent functional limitations. For example, wild type lysozymes are subject to electrostatic sequestration and inactivation by anionic biopolymers in the infected airway. A charge engineered variant of human lysozyme possesses improved antibacterial activity in the presence of disease associated inhibitory molecules718273
additional informationMusca domestica-comparison of the structure, surface charge, dissociation constants, and pH optimum of the fly enzyme with the enzyme from egg white, overview717509
additional informationGallus gallus-the active site of lysozyme contains two catalytic residues, Glu35 and Asp52, which lie in a cleft to the vicinity of the largest pocket and harbor the substrate binding site717672
additional informationHomo sapiens-the modified bovine milk is a possible substitute for human milk718276
additional informationGallus gallus-the reaction follows a Michaelis-Menten mechanism718362

SUBSTRATEPRODUCT                      REACTION DIAGRAMORGANISM UNIPROT ACCESSION NO. COMMENTARY/
Substrate		 LITERATURE/
Substrate		 COMMENTARY/
Product		 LITERATURE/
Product		 Reversibility
r=reversible
ir=irreversible
?=not specified
(GlcNAc)5 + H2O?
show the reaction diagram		Rhea americana--664365--?
(GlcNAc)6 + H2O(GlcNAc)3
show the reaction diagram		Rhea americana--664365and smaller amounts of (GlcNAc)2 and (GlcNAc)4 endo-splitting, hydrolyzes preferentially the third glycosidic linkage from the nonreducing end-?
4-methylumbelliferyl-beta-D-N,N',N''-triacetylchitotrioside + H2O?
show the reaction diagram		Gallus gallus--718362--?
4-methylumbelliferyl-beta-D-N,N',N''-triacetylchitotrioside + H2O?
show the reaction diagram		Musca domestica--717509--?
chitin + H2Osugars
show the reaction diagram		Oncorhynchus mykiss--171041--?
chitin + H2Osugars
show the reaction diagram		Triticum aestivum--171040reducing171040?
chitin + H2Osugars
show the reaction diagram		Saccharopolyspora erythraea-not171059---
chitopentaose + H2O?
show the reaction diagram		Nephtys hombergii--171072--?
chitotetraose + H2Ochitotriose + N-acetylglucosamine
show the reaction diagram		Ruminantia, Bos taurus, Ovis aries--171045-171045?
chitotetraose + H2Ochitotriose + N-acetylglucosamine
show the reaction diagram		Anas platyrhynchos--171050--?
chitotetraose + H2Ochitotriose + N-acetylglucosamine
show the reaction diagram		Cervidae--171045-171045?
chitotetraose + H2Ochitotriose + N-acetylglucosamine
show the reaction diagram		Nephtys hombergii-not171072---
colloidal chitinsugars
show the reaction diagram		Pseudomonas aeruginosa--171095--?
colloidal chitinsugars
show the reaction diagram		Medicago sativa--171096--?
ethylene glycol chitin + H2Osugars
show the reaction diagram		Gallus gallus, Meleagris gallopavo, Homo sapiens--171069--?
ethylene glycol chitin + H2Osugars
show the reaction diagram		Pseudomonas aeruginosa--171095--?
ethylene glycol chitin + H2Osugars
show the reaction diagram		Brassica sp., Streptomyces globisporus--171069--?
ethylene glycol chitin + H2Osugars
show the reaction diagram		Triticum aestivum--171040reducing171040?
ethylene glycol chitin + H2Osugars
show the reaction diagram		Saccharopolyspora erythraea-not171059---
ethylene glycol chitin + H2Osugars
show the reaction diagram		Clostridium acetobutylicum-not171101---
GlcNAcbeta(1-4)GlcNAcbeta(1-4)GlcNAcbeta(1-4)GlcNAcbeta(1-4)GlcNAcbeta + H2OGlcNAcbeta(1-4)GlcNAcbeta(1-4)GlcNAcbeta + (GlcNAc)2
show the reaction diagram		Struthio camelus--697868main products-?
GlcNAcbeta(1-4)GlcNAcbeta(1-4)GlcNAcbeta(1-4)GlcNAcbeta(1-4)GlcNAcbeta + H2OGlcNAcbeta(1-4)GlcNAcbeta(1-4)GlcNAcbeta + ?
show the reaction diagram		Gallus gallus--696840--?
GlcNAcbeta(1-4)GlcNAcbeta(1-4)GlcNAcbeta(1-4)GlcNAcbeta(1-4)GlcNAcbeta(1-4)GlcNAcbeta + H2OGlcNAcbeta(1-4)GlcNAcbeta(1-4)GlcNAcbeta
show the reaction diagram		Anser anserP00718-698655--?
glycol chitin + H2Osugars
show the reaction diagram		Gallus gallus--171035, 171094, 171103--?
glycol chitin + H2Osugars
show the reaction diagram		Homo sapiens--171100--?
glycol chitin + H2Osugars
show the reaction diagram		Bos taurusP80189-171093--?
glycol chitin + H2Osugars
show the reaction diagram		Ovis ariesP80190-171093--?
glycol chitin + H2Osugars
show the reaction diagram		Musca domestica--171102--?
glycol chitin + H2Osugars
show the reaction diagram		Triticum aestivum--171040reducing171040?
glycol chitin + H2Osugars
show the reaction diagram		Saccharopolyspora erythraea-not171059---
N,N',N'',N''',N'''',N'''''-hexaacetylchitohexaose + H2O?
show the reaction diagram		Gallus gallus-eight amino acid residues interact with the N,N',N'',N''',N'''',N'''''-hexaacetylchitohexaose oligomer: Arg73, Gly102, Asn103, Leu56, Ala107, Val109, Ala110, and Lys33680541--?
N,N',N'',N''',N''''-pentaacetylchitopentaose + H2O?
show the reaction diagram		Chelonia mydas--682698--?
N,N',N'',N''',N''''-pentaacetylchitopentaose + H2ON,N'-diacetylchitobiose + p-nitrophenyl beta-D-N',N'',N'''-triacetylchitotriose
show the reaction diagram		Struthio camelus-wild-type protein hydrolyzes N,N',N'',N''',N''''-pentaacetylchitopentaose almost completely on 140 min reaction. N,N',N'',N'''-tetraacetylchitotetraose is is hydrolyzed mainly to N,N'-diacetylchitobiose + p-nitrophenyl beta-D-N',N'',N'''-triacetylchitotriose with much less cleavage into GlcNAc + N,N',N'',N'''-tetraacetylchitotetraose680548--?
N,N',N''-triacetylchitotrioside + H2O?
show the reaction diagram		Musca domestica--681655--?
NodRm-IV + H2ONodRm-II + NodRm-III
show the reaction diagram		Medicago sativa--171096-171096?
NodRm-IV(Ac,S) + H2ONodRm-II + NodRm-III
show the reaction diagram		Medicago sativa--171096-171096?
NodRm-IV(S) + H2ONodRm-II + NodRm-III
show the reaction diagram		Medicago sativa--171096-171096?
NodRm-V(S) + H2ONodRm-II + NodRm-III
show the reaction diagram		Medicago sativa--171096-171096?
p-nitrophenyl-GlcNAcbeta(1-4)GlcNAcbeta(1-4)GlcNAcbeta(1-4)GlcNAcbeta(1-4)GlcNAcbeta + H2O?
show the reaction diagram		Homo sapiens--696869--?
p-nitrophenyl-N,N',N'',N''',N''''-pentaacetylchitopentaose + H2O?
show the reaction diagram		Micrococcus luteus, Liolophura japonica, Omphalius pfeifferi--679934--?
p-nitrophenyl-N,N',N'',N''',N''''-pentaacetylchitopentaose + H2O?
show the reaction diagram		Saxidomus purpuratus--679932--?
peptidoglycan + H2O?
show the reaction diagram		Ovis aries, Cervidae--171045---
peptidoglycan + H2O?
show the reaction diagram		Gallus gallus-Micrococcus lysodeikticus cells679544, 680207, 680255, 681060--?
peptidoglycan + H2O?
show the reaction diagram		Homo sapiens-Micrococcus lysodeikticus cells682197--?
peptidoglycan + H2O?
show the reaction diagram		Micrococcus luteus-Micrococcus lysodeikticus cells679934--?
peptidoglycan + H2O?
show the reaction diagram		Bacillus sp.-Micrococcus lysodeikticus cells679957--?
peptidoglycan + H2O?
show the reaction diagram		Liolophura japonica, Omphalius pfeifferi-Micrococcus lysodeikticus cells679934--?
peptidoglycan + H2O?
show the reaction diagram		Saxidomus purpuratus-Micrococcus lysodeikticus cells679932--?
peptidoglycan + H2O?
show the reaction diagram		Homo sapiens-anti-tumor activity, involvement in host defence, anti-metastatic activity171036---
peptidoglycan + H2O?
show the reaction diagram		Enterobacteria phage T4-cell lysis from within, at the end of latent period, cell lysis from without, at the beginning of infection171052---
peptidoglycan + H2O?
show the reaction diagram		Ruminantia-digestive enzyme171045---
peptidoglycan + H2O?
show the reaction diagram		Lactococcus lactisQ8KKF9AcmB is an N-acetylglucosaminidase autolysin, three-domain modular structure, hydrolyzes peptidoglycans of several Gram-positive bacteria including Lactococcus lactis, AcmB hydrolyzes the peptidoglycan bonds in Bacillus subtilis HR vegetative cells between N-acetylglucosamine and N-acetylmuramic acid thus being an N-acetylglucosaminidase656731--?
peptidoglycan + H2O?
show the reaction diagram		Clostridium phage phi3626-murein hydrolase, highly specific towards cell walls of Clostridium perfringens strains, endolysin Ply3626 has an N-terminal N-acetylmuramoyl-L-alanine amidase domain and a unique C-terminal portion, which might be responsible for the specific lytic range of enzyme654265--?
peptidoglycan + H2O?
show the reaction diagram		Crassostrea virginica-enzyme displays lytic activity against Lactococcus garvieae, Enterococcus sp., Vibrio vulnificus and Escherichia coli. The growth of Aeromonas hydrophila is inhibited only at a high concentration of 0.4 mg/ml. No growth inhibition of Streptococcus iniae and Aeromonas hydrophila664651--?
peptidoglycan + H2O?
show the reaction diagram		Bufo andrewsi-enzyme displays lytic activity against Micrococcus lysodeikticus, Staphylococcus aureus and Escherichia coli664671--?
peptidoglycan + H2O?
show the reaction diagram		Gallus gallus-enzyme is active on extraction of the following bacteria (in order of decreasing activity): Micrococcus lysodeikticus, Salmonella typhimurium, Yersinia enterolitica, Pseudomonas aeruginosa and Escherichia coli665003--?
peptidoglycan + H2O?
show the reaction diagram		Brassica oleracea-enzyme is active on extraction of the following bacteria (in order of decreasing activity): Yersinia enterolitica, Escherichia coli, Micrococcus lysodeikticus, Salmonella typhimurium and Pseudomonas aeruginosa665003--?
peptidoglycan + H2O?
show the reaction diagram		Streptomyces globisporus-enzyme is active on extraction of the following bacteria (in order of decreasing activity): Yersinia enterolitica, Escherichia coli, Pseudomonas aeruginosa, Salmonella typhimurium, Micrococcus lysodeikticus665003--?
peptidoglycan + H2O?
show the reaction diagram		Anser sp.-enzyme is active on extraction of the following bacteria (in order of decreasing activity): Yersinia enterolitica, Pseudomonas aeruginosa, Escherichia coli, Salmonella typhimurium and Micrococcus lysodeikticus665003--?
peptidoglycan + H2O?
show the reaction diagram		Enterobacteria phage T4-enzyme is active on extraction of the following bacteria (in order of decreasing activity): Yersinia enterolitica, Salmonella typhimurium, Micrococcus lysodeikticus, Pseudomonas aeruginosa and Escherichia coli665003--?
peptidoglycan + H2O?
show the reaction diagram		Enterobacteria phage lambda-enzyme is active on extraction of the following bacteria (in order of decreasing activity): Yersinia enterolitica, Salmonella typhimurium, Pseudomonas aeruginosa, Escherichia coli and Micrococcus lysodeikticus665003--?
peptidoglycan + H2O?
show the reaction diagram		Anser sp., Struthio camelus-lyophilized cell wall of Micrococcus luteus664365--?
peptidoglycan + H2O?
show the reaction diagram		Salmo salar-lyophilized cell wall of Micrococcus luteus679139--?
peptidoglycan + H2O?
show the reaction diagram		Rhea americana, Casuarius casuarius-lyophilized cell wall of Micrococcus luteus664365--?
peptidoglycan + H2O?
show the reaction diagram		Gallus gallus-lysis of Micrococcus lysodeikticus cells664351--?
peptidoglycan + H2O?
show the reaction diagram		Chelonia mydas-cell wall of Micrococcus luteus. Tyr34, Tyr45, Pro47, Pro102, and Asn114 are the amino acids contributing to the substrate binding682698--?
peptidoglycan + H2O?
show the reaction diagram		Lactobacillus phage phigaY-LysgaY lysed over 20 heated Gram-positive bacterial species as the substrates, including lactobacilli, lactococci, enterococci, micrococci, and staphylococci680003--?
peptidoglycan + H2O?
show the reaction diagram		Homo sapiens-lytic activity against Micrococcus lysodeikticus677972--?
peptidoglycan + H2O?
show the reaction diagram		Struthio camelus-lytic activity against Micrococcus lysodeikticus680548--?
peptidoglycan + H2O?
show the reaction diagram		Gallus gallus, Homo sapiens-lytic activity against Micrococcus lysodeiktikus cells677858--?
peptidoglycan + H2O?
show the reaction diagram		Gallus gallus-lytic activity with cells of Gram-positive bacteria: Enterococcus faecalis, Bacillus subtilis, Listeria innocua, Staphylococcus aureus and Micrococcus lysodeikticus cells. No activity on Gram-negative bacteria. Pseudomonas aeruginosa, Escherichia coli 0157:H7 and Yersinia enterolytica become sensitive to lysozyme under high pressure. Salmonella typhimurium remains completely insensitive to lysozyme680229--?
peptidoglycan + H2O?
show the reaction diagram		Brassica oleracea-lytic activity with cells of Gram-positive bacteria: Enterococcus faecalis, Bacillus subtilis, Listeria innocua, Staphylococcus aureus and Micrococcus lysodeikticus cells. No activity on Gram-negative bacteria. Pseudomonas aeruginosa, Yersinia enterolytica and Escherichia coli 0157:H7 become sensitive to lysozyme under high pressure. Salmonella typhimurium and Shigella flexneri remain completely insensitive to lysozyme680229--?
peptidoglycan + H2O?
show the reaction diagram		Streptomyces globisporus-lytic activity with cells of Gram-positive bacteria: Enterococcus faecalis, Bacillus subtilis, Listeria innocua, Staphylococcus aureus and Micrococcus lysodeikticus cells. No activity on Gram-negative bacteria. Pseudomonas aeruginosa, Yersinia enterolytica and Escherichia coli become sensitive to lysozyme under high pressure. Salmonella typhimurium and Shigella flexneri remain completely insensitive to lysozyme680229--?
peptidoglycan + H2O?
show the reaction diagram		Enterobacteria phage T4-lytic activity with cells of Gram-positive bacteria: Enterococcus faecalis, Bacillus subtilis, Listeria innocua, Staphylococcus aureus and Micrococcus lysodeikticus cells. No activity on Gram-negative bacteria. Pseudomonas aeruginosa, Yersinia enterolytica and Escherichia coli become sensitive to lysozyme under high pressure. Salmonella typhimurium remains completely insensitive to lysozyme680229--?
peptidoglycan + H2O?
show the reaction diagram		Anser sp.-lytic activity with cells of Gram-positive bacteria: Enterococcus faecalis, Bacillus subtilis, Listeria innocua, Staphylococcus aureus and Micrococcus lysodeikticus cells. No activity on Gram-negative bacteria. Pseudomonas aeruginosa, Yersinia enterolytica and Shigella flexneri become sensitive to lysozyme under high pressure, Salmonella typhimurium and E. coli 0157:H7 remain completely insensitive to lysozyme680229--?
peptidoglycan + H2O?
show the reaction diagram		Enterobacteria phage lambda-lytic activity with cells of Gram-positive bacteria: Enterococcus faecalis, Bacillus subtilis, Listeria innocua, Staphylococcus aureus and Micrococcus lysodeikticus cells. No activity on Gram-negative bacteria. Pseudomonas aeruginosa, Yersinia enterolytica, Shigella flexneri and Escherichia coli become sensitive to lysozyme under high pressure. Salmonella typhimurium remains completely insensitive to lysozyme680229--?
peptidoglycan + H2O?
show the reaction diagram		Pelodiscus sinensis-the enzyme form SSTL A shows lytic activity against several species of bacteria, such as Micrococcus luteus and Vibrio cholerae, but shows only weak activity to Pseudomonas aeruginosa and lacks activity towards Aeromonas hydrophila, the enzyme form SSTL B shows lytic activity against several species of bacteria, such as Micrococcus luteus and Vibrio cholerae, but shows only weak activity to Pseudomonas aeruginosa and lacks activity towards Aeromonas hydrophila679342--?
peptidoglycan + H2O?
show the reaction diagram		Xanthomonas phage Xop411A1BPG9the enzyme is active against both Xanthomonas and Stenotrophomonas maltophilia. Only a minor portion of the Escherichia coli cells is lysed. Cells of Micococcus lysodeikticus, Bacillus subtilis, Agrobacterium tumefaciens, and Psuedomonas fluorescens exhibit no signifiant lysis682650--?
peptidoglycan + H2O?
show the reaction diagram		Chelonia mydas, Amyda cartilaginea-the enzyme shows lytic activity against several species of bacteria, such as Micrococcus luteus and Vibrio cholerae, but shows only weak activity to Pseudomonas aeruginosa and lacks activity towards Aeromonas hydrophila679342--?
peptidoglycan + H2O?
show the reaction diagram		Streptococcus phage B30-the Streptococcus agalactiae bacteriophage B30 endolysin contains three domains: cysteine, histidine-dependent amidohydrolase/peptidase (CHAP), Acm glycosidase, and the SH3b cell wall binding domain. The Acm domain requires the SH3b domain for activity, while the CHAP domain is responsible for nearly all the cell lysis activity677671--?
peptidoglycan + H2ON-acetylaminosaccharides
show the reaction diagram		Staphylococcus aureus--171081--?
peptidoglycan + H2ON-acetylaminosaccharides
show the reaction diagram		Triticum aestivum--171040--?
peptidoglycan + H2ON-acetylaminosaccharides
show the reaction diagram		Oncorhynchus mykiss--171041--?
peptidoglycan + H2ON-acetylaminosaccharides
show the reaction diagram		Enterobacteria phage T4--171052C3 and C6 muropeptides171052?
glycol chitin + H2O?
show the reaction diagram		Gallus gallus--679544, 696840, 698654--?
additional information?-Gallus gallus-Micrococcus lysodeikticus cells171069, 171103, 171106, 171111---
additional information?-Meleagris gallopavo, Homo sapiens-Micrococcus lysodeikticus cells171069---
additional information?-Homo sapiens-Micrococcus lysodeikticus cells171100---
additional information?-Bos taurus-Micrococcus lysodeikticus cells171104---
additional information?-Oryctolagus cuniculus-Micrococcus lysodeikticus cells171108---
additional information?-Canis lupus familiaris-Micrococcus lysodeikticus cells171098---
additional information?-Medicago sativa-Micrococcus lysodeikticus cells171096---
additional information?-Brassica sp., Streptomyces globisporus-Micrococcus lysodeikticus cells171069---
additional information?-Clostridium acetobutylicum-cell walls of Clostridium acetobulyticum, not: Micrococcus cells, beta-N-acetyl chitotetraoside171101---
additional information?-Oncorhynchus mykiss-not: p-nitrophenyl-N-acetylglucosaminide171041---
additional information?-Musca domestica-not: Micrococcus luteus cells171102---
additional information?-Gallus gallus, Homo sapiens, Equus caballus-Micrococcus luteus171109---
additional information?-Ornithodoros moubata-Micrococcus luteus171097---
additional information?-Carica papaya-high chitinase activity171080---
additional information?-Pseudomonas aeruginosa-pyocinogenic: no activity towards intact cells of gram-negative and gram-positive bacteria, lysis of chloroform-killed gram-negative and gram-positive bacteria171058---
additional information?-Enterobacteria phage P22-gram-negative bacteria better substrate than gram-positive bacteria171077---
additional information?-Enterobacteria phage T4-phage T4: e lysozyme more specific than hen egg-white lysozyme, e lysozyme: hydrolysis of murein chains in which N-acetylmuraminic acid is substituted by peptide side chains L-Ala-D-Glu-meso-diaminopimelic acid-D-Ala171052---
additional information?-Bos taurus-often acts as chitinase: EC 3.2.1.14171049---
additional information?-Triticum aestivum-often acts as chitinase: EC 3.2.1.14171040---
additional information?-Lactococcus lactisQ8KKF9AcmB expression is modulated during cell growth, AcmB is not involved in cell separation but contributes to cellular autolysis656731---
additional information?-Larimichthys crocea-LycGL may be involved in antibacterial immune response activated by bacterial vaccine as an accute-phase molecule677863---
additional information?-Ruditapes philippinarum-Glu18 and Asp30 are the catalytic residues of TJL. The catalytic mechanism of TJL is a retaining mechanism that proceeds through a covalent sugar-enzyme intermediate680812---
additional information?-Bacillus sp.-lysozyme has inhibitory effects on the proliferation of vascular endothelial cell in vitro677778---
additional information?-Gallus gallus-lysozyme inhibits Clostridium perfringens type A and its alpha-toxin production681709---
additional information?-Homo sapiens, Bos taurus-lysozyme is able to kill Entamoeba histolytica trophozoites679303---
additional information?-Musca domestica-the enzyme shows lytic activity towards Micrococcus lysodeikticus681655---
additional information?-Penaeus monodonQ8IT75enzyme exhibits potent lytic activities against fish pathogens700107---
additional information?-unidentified phageQ859R8enzyme lyses specifically Thermus aquaticus cells, with 79% activity on Thermus fhermophilus HB8 and 76% activity on Thermus filífformis696020---
additional information?-Homo sapiensP61626lysozyme and its derived peptides are able to bind biotin-labeled pUC19 plasmid DNA. The nonpeptide RAWVAWRNR, amino acids 107-115 of lysozyme, binds DNA with a KD value comparable to histones. Binding results in conformational changes. Lysozyme may represent part of the innate immune system with a very broad protective spectrum695659---
additional information?-Musca domesticaB3GQR5recombinant enzyme displays inhibitory activity against Gram-negative and Gram-positive bacteria699304---
additional information?-Gallus gallus-measurement of activity by lytic activity against Micrococcus luteus698654---
additional information?-Gallus gallus-antimicrobial activities of lysozyme derivatives are tested against Staphylococcus aureus ATCC 121002 and Escherichia coli ATCC 29998, as gram-positive and gram-negative representatives, respectively. The enzyme is activa against Staphylococcus aureus, but only poorly against Escherichia coli, overview, a suspension of Micrococcus lysodeikticus is used as a substrate718309---
additional information?-Homo sapiensQ86SG7a suspension of Micrococcus lysodeikticus is used as a substrate for HLysG2718120---
additional information?-Enterobacteria phage T4-cell walls of Micrococcus lysodeikticus, are a substrate, while those of Xanthomonas campestris pv. malvacearum and Xanthomonas oryzae pv. oryzae are no substrates718395---
additional information?-Gallus gallus-interaction between gold nanorods and lysozyme as moddel protein, the enzyme retains a high fraction of its native structure with a slight increase in the helical content at the expense of beta-turns. Comparison of the gold nanorod treated lysozyme with free enzyme reveals higher thermodynamic stability under denaturing condition. The enzyme's integrity gains more conformational stability in the vicinity of gold nanorods while its lytic activity does not show any undesirable change717672---
additional information?-Homo sapiens-lysis of Micrococcus luteus bacteria, the double mutant lyses bacteria effectively at alginate, mucin and DNA concentrations that inactivate wild-type enzyme718273---
additional information?-Gallus gallus-Micrococcus luteus cells in the exponential growth phase are used as substrate717301---
additional informationadditional information-Pseudomonas phage phiKZQ8SD18cleaves the glycosidic linkage between N-acetylmuramoyl and N-acetylglucosaminyl residues683684formation of a 1,6-anhydromuramoyl product--

NATURAL SUBSTRATESNATURAL PRODUCTSREACTION DIAGRAMORGANISM UNIPROT ACCESSION NO.COMMENTARY SUBSTRATELITERATURE
(Substrate)		COMMENTARY PRODUCTLITERATURE
(Product)
peptidoglycan + H2O?
show the reaction diagram		Ovis aries, Cervidae--171045--
peptidoglycan + H2O?
show the reaction diagram		Homo sapiens-anti-tumor activity, involvement in host defence, anti-metastatic activity171036--
peptidoglycan + H2O?
show the reaction diagram		Enterobacteria phage T4-cell lysis from within, at the end of latent period, cell lysis from without, at the beginning of infection171052--
peptidoglycan + H2O?
show the reaction diagram		Ruminantia-digestive enzyme171045--
additional information?-Lactococcus lactisQ8KKF9AcmB expression is modulated during cell growth, AcmB is not involved in cell separation but contributes to cellular autolysis656731--
additional information?-Larimichthys crocea-LycGL may be involved in antibacterial immune response activated by bacterial vaccine as an accute-phase molecule677863--
additional information?-Penaeus monodonQ8IT75enzyme exhibits potent lytic activities against fish pathogens700107--
additional information?-unidentified phageQ859R8enzyme lyses specifically Thermus aquaticus cells, with 79% activity on Thermus fhermophilus HB8 and 76% activity on Thermus filífformis696020--
additional information?-Homo sapiensP61626lysozyme and its derived peptides are able to bind biotin-labeled pUC19 plasmid DNA. The nonpeptide RAWVAWRNR, amino acids 107-115 of lysozyme, binds DNA with a KD value comparable to histones. Binding results in conformational changes. Lysozyme may represent part of the innate immune system with a very broad protective spectrum695659--
additional information?-Musca domesticaB3GQR5recombinant enzyme displays inhibitory activity against Gram-negative and Gram-positive bacteria699304--
additional information?-Gallus gallus-antimicrobial activities of lysozyme derivatives are tested against Staphylococcus aureus ATCC 121002 and Escherichia coli ATCC 29998, as gram-positive and gram-negative representatives, respectively. The enzyme is activa against Staphylococcus aureus, but only poorly against Escherichia coli, overview718309--
additional informationadditional information-Pseudomonas phage phiKZQ8SD18cleaves the glycosidic linkage between N-acetylmuramoyl and N-acetylglucosaminyl residues683684formation of a 1,6-anhydromuramoyl product-

COFACTORORGANISM UNIPROT ACCESSION NO.COMMENTARYLITERATUREIMAGE
additional informationTriticum aestivum-no metal cofactor required171040-

METALS and IONS ORGANISM UNIPROT ACCESSION NO.COMMENTARY LITERATURE
Ag+Staphylococcus aureus-activates171081
Ca2+Staphylococcus aureus-activates171081
Ca2+Canis lupus familiaris-binding sites171098
Ca2+Homo sapiens-binding sites171100, 171109, 171110
Ca2+Equus caballus-binding sites171109
Ca2+Equus caballus-required, strong temperature dependences of apparent affinities to Ca2+ due to low thermal stability of the apoform, the primary Mg2+ site of the enzyme is different from its Ca2+-binding site, Ca2+-binding sites are generally able to bind Mg2+., overview718376
CaCl2Crassostrea virginica-activates, maximal activity at 0.035 M664651
Co2+Gallus gallus-increases the formation of lysozyme dimers680207
Cu2+Pseudomonas aeruginosa-activates171095
Cu2+Bacillus sp.-0.01 mM, activity is enhanced to 128% of control679957
Cu2+Xanthomonas phage Xop411A1BPG91.0 mM, activity is increased by 54%682650
Mg2+Enterobacteria phage T4-no effect: ghost lysozyme171052
Mg2+Enterobacteria phage T4-increases activity in phage T4 e lysozyme171053
Mg2+Equus caballus-required, strong temperature dependences of apparent affinities to Mg2+ due to low thermal stability of the apoform and relatively high unfavorable enthalpies of Mg2+ association, the primary Mg2+ site of the enzyme is different from its Ca2+-binding site. The Ca2+/Mg2+ selectivity of Mg2+-site of EQL is below an order of magnitude. The enzyme exhibits a distinct Mg2+-specific site, probably arising as an adaptation to the extracellular environment, overview718376
MgCl2Crassostrea virginica-activates, maximal activity at 0.035 M664651
MnGallus gallus-the reaction of the covalent (Mn(CO)3(H2O)2)+–lysozyme adduct with NiS4 and NiN2S2 complexes generates binuclear Ni–Mn complexes679189
Na+Homo sapiensQ86SG7activates, best at 75 mM718120
NaClStaphylococcus aureus-activates171081
NaClCrassostrea virginica-activity increases as the NaCl concentration is increased from 0 to 0.1 M and then decreases from its maximum activity at 0.1 M NaCl with further increase in NaCl concentrations664651
NiGallus gallus-the reaction of the covalent (Mn(CO)3(H2O)2)+–lysozyme adduct with NiS4 and NiN2S2 complexes generates binuclear Ni–Mn complexes679189
Zn2+Bacillus sp.-0.01 mM, activity is enhanced to 135% of control679957

INHIBITORSORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE IMAGE
(GlcNAc)2Gallus gallus--171092 2D-image
(GlcNAc)3Gallus gallus--171092 2D-image
(GlcNAc)3Bos taurusP80189-171093 2D-image
(GlcNAc)3Ovis ariesP80190-171093 2D-image
(GlcNAc)3Oryctolagus cuniculus--171108 2D-image
2-mercaptoethanolPseudomonas aeruginosa--171095 2D-image
4-hexylresorcinolGallus gallus-activates at low concentrations, up to 10-15 molcules of hexylresorcinol per protein globule, but inhibits at higher concentrations, at above 100 molecules of hexylresorcinol per protein globule the activity is abolished717301 2D-image
5-[(4,6-dichloro-1,3,5-triazin-2-yl)amino]-4-hydroxy-3-[(E)-phenyldiazenyl]naphthalene-2,7-disulfonateGallus gallus-i.e. brilliant red. Non-covalent interaction with formation of multiple complexes such as lysozyme(brilliant red)17 at pH 2.0, lysozyme(brilliant red)15 at pH 3.3, lysozyme(brilliant red)12 at pH 4.4. Two-step binding model, in which one or two brilliant red molecules enter the hydrophobic outer surface of lysozyme. Binding results in change of lysozyme conformation and in its inhibition695524 2D-image
Ag+Bacillus sp.-0.01 mM, 7% inhibition679957 2D-image
Ag2+Clostridium acetobutylicum--171101 2D-image
AgNO3Triticum aestivum--171040 2D-image
alginateHomo sapiens-inactivation of the wild-type enzyme at high concentrations718273 2D-image
Bacillus subtilis DNAGallus gallus-in presence of 0-50 mM NaCl171069-
chitotetraoseBos taurus, Cervidae, Ovis aries, Ruminantia--171045 2D-image
Co(NO3)2Lactobacillus phage phigaY-10 mM680003 2D-image
CoCl2Lactobacillus phage phigaY-10 mM680003 2D-image
CoCl2Xanthomonas phage Xop411A1BPG91 mM682650 2D-image
CuSO4Staphylococcus aureus--171081 2D-image
CuSO4Lactobacillus phage phigaY-10 mM680003 2D-image
dithiothreitolPseudomonas aeruginosa--171095 2D-image
DNAGallus gallus-DNA from herring sperm, in presence of 0-50 mM NaCl171069 2D-image
DNAHomo sapiens-inactivation of the wild-type enzyme at high concentrations718273 2D-image
EDTAStaphylococcus aureus-above 0.1 mM171081 2D-image
EDTAXanthomonas phage Xop411A1BPG9at 10 and 20 mM causes 15% and 43% reduction of the enzyme activity682650 2D-image
F-actinHomo sapiens-inhibition of the wild-type enzyme718273-
Fe3+Clostridium acetobutylicum--171101 2D-image
FeCl3Xanthomonas phage Xop411A1BPG91 mM682650 2D-image
glucosamineClostridium acetobutylicum--171101 2D-image
glutathionePseudomonas aeruginosa--171095 2D-image
glycol chitosanTriticum aestivum--171040-
HewliGallus gallus, Homo sapiens, Meleagris gallopavo--171069-
Hg2+Clostridium acetobutylicum--171101 2D-image
HgCl2Triticum aestivum--171040 2D-image
histamineTriticum aestivum--171040 2D-image
histamineNephtys hombergii--171072 2D-image
histamineFicus sp.--171086 2D-image
Human serum albuminGallus gallus-the catalytic rate constant decreases tenfold when the albumin concentration increases, while the Michaelis constant remains almost constant in the albumin concentration range employed. Theoretical modeling of the structure of the human serum albumin-lysozyme complex shows that the Glu35 and Asp52 residues located in the active site of lysozyme are oriented toward the human serum albumin surface. This conformation will inactivate lysozyme molecules bound to human serum albumin, molecular dynamic calculations, overview718362-
IClCarica papaya--171080 2D-image
inhibitor of vertebrate lysozymeAnser anser-Escherichia coli inhibitor of vertebrate lysozyme. Electrostatic interactions makes a dominant contribution to inhibition. Weaker binding mode between Ivy and goose lysozyme compared to hen lysozyme699629-
inhibitor of vertebrate lysozymeGallus gallus-i.e. Escherichia coli inhibitor of vertebrate lysozyme. Electrostatic interactions makes a dominant contribution to inhibition. Weaker binding mode between Ivy and goose lysozyme compared to hen lysozyme699629-
IvyAnser sp., Enterobacteria phage T4, Gallus gallus-lysozyme inhibitor from Escherichia coli, strong inhibition664786-
KClEnterobacteria phage P22--171077 2D-image
lipoproteinGallus gallus-lipoprotein in bound form, in presence of 0-5 mM NaCl171069-
MgCl2Enterobacteria phage P22--171077 2D-image
MgCl2Pseudomonas aeruginosa--171095 2D-image
MliCGallus gallus-i.e. membrane bound lysozyme inhibitor of C-type lysozyme, crystallization data in complex with chicken egg white lysozyme. The invariant loop of MliC plays a crucial role in the inhibition by its insertion to the active site cleft of the lysozyme, where the loop forms hydrogen and ionic bonds with the catalytic residues696021-
MliCGallus gallus-i.e. membrane bound lysozyme inhibitors of c-type lysozyme, isolated from Escherichia coli and Pseudomonas aeruginosa, possess lysozyme inhibitory activity and confer increased lysozyme tolerance upon expression in Escherichia coli. Related to a group of proteins with a common conserved COG3895 domain700911-
Mn2+Pseudomonas aeruginosa--171095 2D-image
mucinHomo sapiens-inactivation of the wild-type enzyme at high concentrations718273-
N,N',N''-triacetylchitotrioseGallus gallus-competitive. Preincubation at neutral pH impairs aggregation of lysozyme and fibrillogenesis at pH 12.2. Lysozyme-chitotriose complex at pH 12.2 displays reduced thioflavin T and 8-anilino-1-naphthalene sulfonic acid fluorescence, small oligomers but no amyloid fibrils, absence of large aggregates, marginally more helical content, and more than 70% of enzymatic activity after 24 h696471 2D-image
N-acetylglucosamineBos taurus--171049 2D-image
N-acetylglucosamineNilssonia gangetica--171061 2D-image
N-acetylglucosamineNephtys hombergii--171072 2D-image
N-acetylglucosamineBrassica sp.--171079 2D-image
N-acetylglucosamineFicus sp.--171086 2D-image
N-acetylglucosamineGallus gallus--171092 2D-image
N-acetylglucosamineClostridium acetobutylicum--171101 2D-image
N-acetylmuramic acidBos taurus--171049 2D-image
N-bromosuccinimideCarica papaya-pH 4171080 2D-image
NaClEnterobacteria phage P22--171077 2D-image
NiClXanthomonas phage Xop411A1BPG91 mM682650 2D-image
NiSO4Lactobacillus phage phigaY-10 mM680003 2D-image
Nuclear lysozyme inhibitorRattus norvegicus-other subcellular lysozymes except nuclear are unaffected171054-
PliCGallus gallus-i.e. periplasmic lysozyme inhibitor of c-type lysozyme, isolated by affinity chromatography from a periplasmic extract of Salmonella enteritidis and related to a group of proteins with a common conserved COG3895 domain700911-
PliIRuditapes philippinarum-periplasmic lysozyme inhibitor of the I-type lysozyme from Aeromonas hydrophila has a high affinity for I-type lysozyme, but does not bind or inhibit vertebrate C- or G-type lysozymes708061-
poly-alpha,D-Na-glutamateGallus gallus-in presence of 0-100 mM NaCl171069-
poly-gamma,D-Na-glutamateGallus gallus-in presence of 0-100 mM NaCl171069-
poly-L-lysineTriticum aestivum--171040 2D-image
porcine gastric mucinGallus gallus, Homo sapiens-inhibits activity of lysozyme in solution in a pH-dependent manner. The amount of inhibition is dependent on mucin concentration, incubation time and temperature, and the structural integrity of the mucin677858-
potassium hyaluronateGallus gallus-in presence of 0-5 mM NaCl171069 2D-image
RNAGallus gallus-yeast RNA in presence of 0-50 mM NaCl171069 2D-image
SDSStaphylococcus aureus--171081 2D-image
Sodium citrateStaphylococcus aureus-above 0.1 M171081 2D-image
Zn(NO3)2Lactobacillus phage phigaY-10 mM680003 2D-image
ZnCl2Triticum aestivum--171040 2D-image
ZnCl2Pseudomonas aeruginosa--171095 2D-image
ZnCl2Lactobacillus phage phigaY-10 mM680003 2D-image
Mn2+Bacillus sp.-0.01 M, 17% inhibition679957 2D-image
additional informationAnser sp.-as yet unknown lysozyme inhibitors may exist in some Gram-negative bacteria, including Salmonella typhimurium and Pseudomonas aeruginosa665003-
additional informationBrassica oleracea-as yet unknown lysozyme inhibitors may exist in some Grame-negative bacteria, including Salmonella typhimurium and Pseudomonas aeruginosa665003-
additional informationEnterobacteria phage lambda, Enterobacteria phage T4, Gallus gallus, Streptomyces globisporus-as yet unknown lysozyme inhibitors may exist in some Gram-negative bacteria, including Salmonella typhimurium and Pseudomonas aeruginosa665003-
additional informationOenococcus phage fOg44-bacterial membrane proton motive force regulates the lytic activity of the secreted endolysin Lys44 from Oenococcus oeni phage fOg44. Cytoplasmic membrane voltage dissipation is necessary but not sufficient for the full sensitization of cells to Lys44680524-
additional informationHomo sapiensP61626lysozyme and its derived peptides are able to bind biotin-labeled pUC19 plasmid DNA. The nonpeptide RAWVAWRNR, amino acids 107-115 of lysozyme, binds DNA with a KD value comparable to histones. Binding results in conformational changes695659-
additional informationSalmo salar-Escherichia coli inhibitor of vertebrate lysozyme, Ivy, is not inhibitory699629-
additional informationGallus gallus-study on the inhibitory effect on the enzymatic activity of lysozyme of a number of peptides each containing about 10 amino acids and overlapping exhaustively the protein sequence. A small fraction of them are able to inhibit the biological activity of the protein with micromolar efficiency. The peptide displaying the same sequence of segment 91-100 of the protein, and essentially corresponding to the last three turns of helix C, is the most efficient. The inhibitory mechanism is nonconventional. Local elementary structures formed in the denatured state, drive the folding process and selected peptides compete with these structures in binding complementary regions of the protein, preventing the formation of the native state701132-
additional informationGallus gallus-interaction with gold nanorods slightly decrease the enzyme activity, most at 25 nM, less at 100 nM717672-

ACTIVATING COMPOUNDORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE IMAGE
4-hexylresorcinolGallus gallus-activates at low concentrations, up to 10-15 molcules of hexylresorcinol per protein globule, but inhibits at higher concentrations, at above 100 molecules of hexylresorcinol per protein globule the activity is abolished717301 2D-image
5-methylresorcinolGallus gallus-interacts with the surface of lysozyme directly, not via water hydrogen bonds. This leads to a decrease in the denaturation temperature and an increase in the amplitude of equilibrium fluctuations, allowing it to be a powerful activator717301-
Protein disulfide isomeraseGallus gallus-enhances activity of the activity of renatured lysozyme680954-
TRAPGallus gallus-i.e. target of RNAIII activating protein , membrane-associated protein from Staphylococcus aureus. TRAP can specifically bind lysozyme and lysostaphin through its C-terminus and enhance lysozymal activities in vitro683018-
cholineStreptococcus pneumoniae-the cell wall binding module is intrinsically unstable, and the ultimate folding and stabilization of the active, monomeric form of the enzyme relies on choline binding. Complex formation proceeds in a rather slow way, and all sites behave as equivalent. Coupling between choline binding and folding indicates a high conformational plasticity that could correlate with the unusual alternation of short and long choline-binding repeats present in this enzyme. It can contribute to regulate enzymic activity698818 2D-image
additional informationEnterobacteria phage T4-practically inactive in absence of Triton X-100, hydrolysis of murein catalysed only when in contact with lipophilic components171048-
additional informationunidentified phageQ859R8no activation by 2-mercaptoethanol696020-

KM VALUE [mM]KM VALUE [mM] MaximumSUBSTRATEORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE IMAGE
0.0008-4-methylumbelliferyl-beta-D-N,N',N''-triacetylchitotriosideGallus gallus-human serum albumin-bound enzyme, pH 5.2, 37°C718362 2D-image
8.33-p-nitrophenyl-N,N',N'',N''',N''''-pentaacetylchitopentaoseLiolophura japonica--679934 2D-image
0.001-4-methylumbelliferyl-beta-D-N,N',N''-triacetylchitotriosideGallus gallus-free enzyme, pH 5.2, 37°C718362 2D-image
additional information-additional informationGallus gallus-Michaelis-Menten curve of lysozyme in the presence and absence of gold nanorods717672-
additional information-additional informationGallus gallus-the reaction follows a Michaelis-Menten mechanism718362-
additional information-additional informationEquus caballus-binding constants and thermodynamics of Ca2+ and Mg2+ binding, overview718376-

TURNOVER NUMBER [1/s] TURNOVER NUMBER MAXIMUM[1/s] SUBSTRATEORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE IMAGE
0.015-p-nitrophenyl-GlcNAcbeta(1-4)GlcNAcbeta(1-4)GlcNAcbeta(1-4)GlcNAcbeta(1-4)GlcNAcbetaHomo sapiens--696869-
0.076-p-nitrophenyl-N,N',N'',N''',N''''-pentaacetylchitopentaoseLiolophura japonica--679934 2D-image

kcat/KM VALUE [1/mMs-1]kcat/KM VALUE [1/mMs-1] MaximumSUBSTRATEORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE IMAGE
No entries in this field

Ki VALUE [mM]Ki VALUE [mM] MaximumINHIBITORORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE IMAGE
No entries in this field

IC50 VALUE [mM]IC50 VALUE [mM] MaximumINHIBITORORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE IMAGE
No entries in this field

SPECIFIC ACTIVITY [µmol/min/mg] SPECIFIC ACTIVITY MAXIMUM ORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE
0.085-Pseudomonas aeruginosa-FII171095
0.103-Pseudomonas aeruginosa-FI171095
0.387-Liolophura japonica-substrate: p-nitrophenyl-N,N',N'',N''',N''''-pentaacetylchitopentaose679934
2.98-Micrococcus luteus-substrate: p-nitrophenyl-N,N',N'',N''',N''''-pentaacetylchitopentaose679934
4.32-Omphalius pfeifferi-substrate: p-nitrophenyl-N,N',N'',N''',N''''-pentaacetylchitopentaose679934
31050-unidentified phageQ859R8pH 7.0, 70°C696020
additional information-Triticum aestivum--171040
additional information-Oncorhynchus mykiss-139.8 1/min * mg: decrease in absorbance171041
additional information-Bos taurus, Cervidae, Ovis aries, Ruminantia--171045
additional information-Bos taurus--171049
additional information-Anas platyrhynchos--171050
additional information-Streptococcus pneumoniae--171051
additional information-Rattus norvegicus--171054
additional information-Gallus gallus--171057
additional information-Saccharopolyspora erythraea--171059
additional information-Nilssonia gangetica--171061
additional information-Ceratitis capitata--171065
additional information-Homo sapiens--171066
additional information-unidentified phage--171073
additional information-Equus caballus--171074
additional information-Enterobacteria phage P22--171077
additional information-Papio cynocephalus--171078
additional information-Staphylococcus aureus--171081
additional information-Homo sapiens--171085
additional information-Enterobacteria phage lambda--171087
additional information-Homo sapiens--171088
additional information-Bos taurusP80189-171093
additional information-Ovis ariesP80190-171093
additional information-Medicago sativa--171096
additional information-Ornithodoros moubata--171097
additional information-Clostridium acetobutylicum--171101
additional information-Musca domestica--171102
additional information-Bos taurus--171104
additional information-Oryctolagus cuniculus--171108
additional information-Crassostrea virginica--664651
additional information-Gallus gallus--666704
additional information-Amyda cartilaginea-63 units per mg. One unit is defined as the amount of enzyme causing a decrease of 0.1 absorbance unit at 540 nm in 3 min of reaction at 25°C679342
additional information-Chelonia mydas-58 units per mg. One unit is defined as the amount of enzyme causing a decrease of 0.1 absorbance unit at 540 nm in 3 min of reaction at 25°C679342
additional information-Pelodiscus sinensis-isoenzyme SSTL A: 45 units per mg. One unit is defined as the amount of enzyme causing a decrease of 0.1 absorbance unit at 540 nm in 3 min of reaction at 25°C; isoenzyme SSTL B: 85 units per mg. One unit is defined as the amount of enzyme causing a decrease of 0.1 absorbance unit at 540 nm in 3 min of reaction at 25°C679342
additional information-Gallus gallus-one unit lysozyme activity is defined as the amount of enzyme causing a decrase of 0.001 optical density value per minute at 25°C and pH 7.0. Specific activity of the eluted lysozyme (62580 U/mg) is higher than that obtained with a commercially available pure lysozyme Sigma (60000 U/mg)681060
additional information-Xanthomonas phage Xop411A1BPG97400 U/mg. One unit of enzyme is defined as the amounts that caused the decrease of 0.001 units of absorbance at 550 nM per min682650

pH OPTIMUMpH MAXIMUMORGANISM UNIPROT ACCESSION NO. COMMENTARYLITERATURE
3.5-Clostridium acetobutylicum--171101
4-Saccharopolyspora erythraea--171059
4-Lactococcus lactisQ8KKF9assay at656731
4-Rhea americana-substrate: (GlcNAc)5664365
4-Musca domestica-lytic activity towards Micrococcus lysodeikticus681655
4.55.5Brassica sp.--171079
4.7-Musca domestica-substrate: N,N',N''-triacetylchitotrioside681655
55.5Gallus gallus--680207
57Gallus gallus-assay at717301
58Bos taurus, Cervidae, Ovis aries--171045
5-Bos taurus, Ruminantia--171045
5-Bos taurus--171049
5-Musca domestica--171102
5-Casuarius casuarius-substrate: lyophilized cell wall of Micrococcus luteus664365
5.2-Salmo salar-at ionic strength 0.1679139
5.2-Saxidomus purpuratus--679932
5.2-Micrococcus luteus, Omphalius pfeifferi--679934
5.2-Gallus gallus-assay at718362
5.56Enterobacteria phage T4--171052
5.56Crassostrea virginica--664651
5.5-Oncorhynchus mykiss--171041
5.5-Bos taurusP80189assay at171093
5.5-Ovis ariesP80190assay at171093
5.5-Gallus gallus--171111
5.5-Anser sp.-substrate: lyophilized cell wall of Micrococcus luteus664365
5.9-Homo sapiens-wild-type enzyme, lytic activity against Micrococcus lysodeikticus677972
67unidentified phage--171073
67Homo sapiens-the optimal pH of rHLZ varies with salt concentration of the buffer, recombinant enzyme718276
69.4Staphylococcus aureus--171081
6-Triticum aestivum--171040
6-Enterobacteria phage T4--171048
6-Streptococcus pneumoniae--171051
6-Ornithodoros moubata--171097
6-Gallus gallus-lysis of Micrococcus lysodeikticus cells664351
6-Rhea americana, Struthio camelus-substrate: lyophilized cell wall of Micrococcus luteus664365
6-Enterobacteria phage phiKMV--664563
6-Bufo andrewsi--664671
6-Amyda cartilaginea-ionic strength 0.1679342
6-Chelonia mydas-dual pH-optimum at pH 6.0 and 8.0, ionic strength 0.1679342
6-Pelodiscus sinensis-isoenzyme SSTL A, ionic strength 0.1; isoenzyme SSTL B, ionic strength 0.1679342
6-Homo sapiens-native enzyme and mutant enzyme _K1insN682197
6-Penaeus monodonQ8IT75-700107
6-Homo sapiensQ86SG7recombinant enzyme718120
6.2-Gallus gallus-assay at717672
6.4-Pseudomonas aeruginosa--171058
6.4-Homo sapiens--171088
6.4-Liolophura japonica--679934
6.5-Oryctolagus cuniculus--171055
6.5-Ceratitis capitata--171065
6.5-Bacillus sp.--677778
6.5-Homo sapiens-two-active site lysozyme, lytic activity against Micrococcus lysodeikticus677972
6.5-Bacillus sp.-lytic activity towards Micrococcus lysodleikticus679957
6.5-Lactobacillus phage phigaY--680003
6.6-Xanthomonas phage Xop411A1BPG9the optimal assay conditions determined for the recombinant His-tagged protein are in 0.1M potassium phosphate buffer, pH 6.6 containing 1 mM CuCl2 at 25°C682650
6.8-Salmo salar-at ionic strength 0.03679139
78Enterobacteria phage P22--171077
7-Pseudomonas aeruginosa-FII171095
7-Bos taurus--171104
7-Homo sapiens-mutant _K1insK682197
7-Homo sapiens-assay at718273
7-Gallus gallus-assay at718309
7.2-unidentified phage--171073
7.58.5unidentified phage--171073
7.5-Nilssonia gangetica--171061
7.6-Enterobacteria phage T4--171052
8-Pseudomonas aeruginosa-FI171095
8-Chelonia mydas-dual pH-optimum at pH 6.0 and 8.0, ionic strength 0.1679342
additional information-Musca domestica-the acidic pH optimum for MdL2 and MdL1 activities upon methylumbelliferylchitotrioside is determined by the presence of N46, S106 and T107 in the environment of their catalytic residues, which favors pKas reduction. The acidic pH optimum upon bacterial walls is determined by a low concentration of positive charges on the MdL2 and MdL1 surfaces717509

pH RANGEpH RANGE MAXIMUMORGANISM UNIPROT ACCESSION NO.COMMENTARYLITERATURE
2.57Clostridium acetobutylicum--171101
2.58Saccharopolyspora erythraea--171059
2.58.5Enterobacteria phage T4--171052
35Rhea americana-pH 3: about 65% of maximal activity, pH 5: about 40% of maximal activity, substrate: (GlcNAc)5664365
37Bos taurus--171049
38Ceratitis capitata--171065
39Triticum aestivum--171040
3.34.7Musca domestica-pH 3.3: about 70% of maximal activity, pH 4.7: about 50% of maximal activity, substrate: N,N',N''-triacetyl chitotrioside681655
3.46.5Musca domestica-pH 3.4: about 40% of maximal activity, pH 6.5: about 40% of maximal activity, lytic activity towards Micrococcus lysodeikticus681655
3.57Brassica sp.--171079
47Musca domestica--171102
48Oncorhynchus mykiss--171041
48.5Enterobacteria phage T4--171048
4.46.4Micrococcus luteus-pH 4.4 and pH 6.4: more than 50% of maximal activity679934
4.55.5Casuarius casuarius-pH 4.5: about 60% of maximal activity, pH 5.5: about 70% of maximal activity, substrate: lyophilized cell wall of Micrococcus luteus664365
4.56Salmo salar-pH 4.5: about 40% of maximal activity, pH 6.0: about 65% of maximal activity, at ionic strength 0.1679139
4.58Bacillus sp.-pH 4.5: about 60% of maximal activity, pH 8.0: about 60% of maximal activity679957
4.58.5Oryctolagus cuniculus--171055
4.59.5Nilssonia gangetica--171061
4.59.5Staphylococcus aureus--171081
4.85.6Omphalius pfeifferi-pH 4.8 and pH 5.6: more than 50% of maximal activity679934
4.86.2Saxidomus purpuratus-more than 50% activity in the pH range679932
510Enterobacteria phage P22--171077
510Pseudomonas aeruginosa-FII171095
56.5Anser sp.-pH 5: about 60% of maximal activity, pH 6.5: about 50% of maximal activity, substrate: lyophilized cell wall of Micrococcus luteus664365
56.5Struthio camelus-pH 5: about 45% of maximal activity, pH 6.5: about 50% of maximal activity, substrate: lyophilized cell wall of Micrococcus luteus664365
57Gallus gallus--171111
57Gallus gallus-pH 5.0: wild-type enzyme shows about 80% of maximal activity, S6K-lysozyme and S7-lysozyme shows about 60% of maximal activity, pH 7.0: about 40% of maximal activity, wild-type enzyme, S6K-lysozyme and S7-lysozyme, lysis of Micrococcus lysodeikticus cells664351
57Amyda cartilaginea-pH 5.0: about 50% of maximal activity, pH 7.0: about 90% of maximal activity, ionic strength 0.1679342
57Pelodiscus sinensis-pH 5.0: about 45% of maximal activity, pH 7.0: about 75% of maximal activity, isoenzyme SSTL B, ionic strength 0.1; pH 5.0: about 60% of maximal activity, pH 7.0: about 35% of maximal activity, isoenzyme SSTL A, ionic strength 0.1679342
57.5Crassostrea virginica-60% of maximal activity within the range pH 5.0-7.5664651
57.5Bufo andrewsi-pH 5.0: about 75% of maximal activity, pH 7.5: about 40% of maximal activity664671
59Pseudomonas aeruginosa--171058
59Homo sapiens-activity range, recombinant enzyme718276
5.38Liolophura japonica-pH 5.3 and pH 8.0: more than 50% of maximal activity679934
5.47.2Homo sapiens-wild-type and two-active site lysozyme both retain over 80% activity as determined by assaying the lysis of Micrococcus lysodeikticus cells over a pH range of 5.3 to 7.2677972
5.57Oryctolagus cuniculus--171108
67Xanthomonas phage Xop411A1BPG9pH 6.0: about 60% of maximal activity, pH 7.0: about 55% of maximal activity682650
69Pseudomonas aeruginosa-FI171095
6.57.5Salmo salar-pH 6.5: about 55% of maximal activity, pH 7.5: about 20% of maximal activity, at ionic strength 0.03679139
6.58.5Homo sapiens-from pH 6.5-8.5, the rising of the pH results in decrease in lytic activity of native enzyme and mutant _K1insK, but not _K1insK682197
additional information-Lactococcus lactisQ8KKF9active at acidic pH656731

TEMPERATURE OPTIMUMTEMPERATURE OPTIMUM MAXIMUMORGANISM UNIPROT ACCESSION NO.COMMENTARYLITERATURE
25-Xanthomonas phage Xop411A1BPG9the optimal assay conditions determined for the recombinant His-tagged protein are in 0.1M potassium phosphate buffer, pH 6.6 containing 1 mM CuCl2 at 25°C682650
25-Homo sapiens-assay at718273
3040Struthio camelus-substrate: lyophilized cell wall of Micrococcus luteus664365
30-Streptococcus pneumoniae--171051
30-Bacillus sp.--677778
30-Salmo salar--679139
30-Homo sapiensQ86SG7recombinant enzyme718120
35-Bacillus sp.-lytic activity towards Micrococcus lysodleikticus679957
3742Gallus gallus-assay at717301
37-Staphylococcus aureus--171081
37-Clostridium phage phi3626-assay at654265
37-Lactococcus lactisQ8KKF9assay at656731
37-Lactobacillus phage phigaY--680003
37-Gallus gallus-assay at718309, 718362
4045Crassostrea virginica--664651
40-Bos taurusP80189assay at171093
40-Ovis ariesP80190assay at171093
40-Gallus gallus-assay at171094
40-Pseudomonas aeruginosa-FII171095
40-Rhea americana-substrate: lyophilized cell wall of Micrococcus luteus664365
40-Penaeus monodonQ8IT75-700107
40-Homo sapiens-recombinant enzyme718276
45-Oncorhynchus mykiss--171041
50-Brassica sp.--171079
50-Pseudomonas aeruginosa-FI171095
50-Saxidomus purpuratus--679932
50-Liolophura japonica, Micrococcus luteus--679934
60-Triticum aestivum--171040
60-Omphalius pfeifferi--679934

TEMPERATURE RANGE TEMPERATURE MAXIMUM ORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE
550Salmo salar-5°C: about 70% of maximal activity, 50°C: about 40% of maximal activity679139
550Bacillus sp.-5°C: about 55% of maximal activity, 50°C: about 65% of maximal activity679957
1060Crassostrea virginica-10°C: about 60% of maximal activity, 60°C: about 60% of maximal activity664651
1065Oncorhynchus mykiss--171041
1090Triticum aestivum--171040
1570Brassica sp.--171079
2060Rhea americana-20°C: about 95% of maximal activity, 60°C: about 65% of maximal activity, substrate: lyophilized cell wall of Micrococcus luteus664365
2060Struthio camelus-20°C: about 85% of maximal activity, 60°C: about 75% of maximal activity, substrate: lyophilized cell wall of Micrococcus luteus664365
2090Saxidomus purpuratus-20°C: about 50% of maximal activity, 90°C: about 30% of maximal activity679932
2550Xanthomonas phage Xop411A1BPG925°C: maximal activity, 45°C: about 90% of maximal activity, 50°C: about 40% of maximal activity682650

pI VALUEpI VALUE MAXIMUMORGANISM UNIPROT ACCESSION NO.COMMENTARYLITERATURE
-990-Helicoverpa zea-pI is greater than 9.5 as determined by isoelectric focusing665818
4.7-Anopheles gambiaeA4ZWD2, Q7QHB9calculated698287
4.8-Anopheles gambiaeA4ZWD2, Q7QHB9calculated698287
4.9-Lactococcus lactisQ8KKF9sequence calculation656731
6.4-Enterobacteria phage phiKMV-isoelectric focusing664563
6.8-Rhodnius prolixusA9LN31, A9LN32calculated699392
7.7-Musca domesticaB3GQR5calculated699304
7.88-Chlamys farreriQ075V3calculated from sequence681964
8.44-Ruditapes philippinarum-theoretical pI708229
8.5-Rhodnius prolixusA9LN31, A9LN32calculated699392
8.8-Penaeus monodonQ8IT75calculated700107
9.1-Bufo andrewsi-calculated from sequence664671
9.1-Helicoverpa armigeraQ19R28calculated695906
9.3-Bacillus sp.--677778
additional information-Crassostrea virginica-greater than 10664651

SOURCE TISSUE ORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE SOURCE
abomasumBos taurus--171049Manually annotated by BRENDA team
alimentary canalRhodnius prolixusA9LN31, A9LN32; 699392Manually annotated by BRENDA team
cartilageBos taurus--171071, 171104Manually annotated by BRENDA team
cartilageCanis lupus familiaris--171071Manually annotated by BRENDA team
commercial preparationGallus gallus--696414, 699048, 700151, 717301, 717672, 718309Manually annotated by BRENDA team
commercial preparationGallus gallus-purified717036Manually annotated by BRENDA team
eggCeratitis capitata--171065Manually annotated by BRENDA team
eggRhea americana--664365Manually annotated by BRENDA team
eggGallus gallus--709169Manually annotated by BRENDA team
egg whiteGallus gallus--171035, 171038, 171039, 171057, 171062, 171069, 171089, 171092, 171094, 171099, 171103, 171105, 171106, 171107, 171111, 663498, 663508, 663510, 663529, 664786, 665003, 665757, 665993, 666541, 666704, 677858, 678407, 678484, 678844, 679189, 679544, 680207, 680255, 680380, 680541, 680954, 681060, 681598, 681709, 682603, 683018, 695524, 696021, 698409, 699054, 699629, 699858, 700151, 707414, 707830, 708358, 708362, 708795, 708875, 709764, 710026, 710491, 717036, 717301, 717672, 718309, 718362Manually annotated by BRENDA team
egg whiteNilssonia gangetica--171061Manually annotated by BRENDA team
egg whiteAnas platyrhynchos--171083Manually annotated by BRENDA team
egg whiteAnser sp.--171084, 664365, 664786, 665003, 680229Manually annotated by BRENDA team
egg whiteEnterobacteria phage T4--664786Manually annotated by BRENDA team
egg whiteChelonia mydas--679342, 682698Manually annotated by BRENDA team
egg whitePelodiscus sinensis--679342, 698657Manually annotated by BRENDA team
egg whiteAmyda cartilaginea--679342Manually annotated by BRENDA team
egg whiteStruthio camelus--697868Manually annotated by BRENDA team
egg whiteAnser anserP00718-698655, 699629Manually annotated by BRENDA team
eyeHomo sapiensQ86SG7weak enzyme expression in the conjuctival sample, strong expression in the lacrimal gland sample718120Manually annotated by BRENDA team
fat bodyGalleria mellonella-of larvae. 1 h after infection with Pseudomonas aeruginosa, increase in lysozyme content is detecable, with a significant decrease after a prolonged infection time698030Manually annotated by BRENDA team
fat bodyAnopheles gambiaeA4ZWD2, Q7QHB9of adult female; of adult female698287Manually annotated by BRENDA team
fat bodyMusca domesticaB3GQR5-699304Manually annotated by BRENDA team
fat bodyRhodnius prolixusA9LN31, A9LN32; predominant expression after injection of bacteria699392Manually annotated by BRENDA team
gastric juiceBos taurus--171049Manually annotated by BRENDA team
gastric mucosaBos taurus-3 lysozymes c171045Manually annotated by BRENDA team
germTriticum aestivum--171040Manually annotated by BRENDA team
ghostEnterobacteria phage T4--171052Manually annotated by BRENDA team
gillLarimichthys crocea-constitutively expressed677863Manually annotated by BRENDA team
gillPenaeus monodonQ8IT75high mRNA expression700107Manually annotated by BRENDA team
gutOrnithodoros moubata--171097Manually annotated by BRENDA team
heartLarimichthys crocea-constitutively expressed677863Manually annotated by BRENDA team
hemocyteGalleria mellonella-of larvae. 1 h after infection with Pseudomonas aeruginosa, increase in lysozyme content is detecable, with a significant decrease after a prolonged infection time698030Manually annotated by BRENDA team
hemocytePenaeus monodonQ8IT75high mRNA expression700107Manually annotated by BRENDA team
hemolymphHeliothis virescens-larvae171046Manually annotated by BRENDA team
hemolymphCrassostrea virginica-cell-free664651Manually annotated by BRENDA team
hemolymphGalleria mellonella-of larvae. Increase in lysozyme level during the first 30 h after infection with Pseudomonas aeruginosa698030Manually annotated by BRENDA team
hepatopancreasPenaeus monodonQ8IT75high mRNA expression700107Manually annotated by BRENDA team
intestineLarimichthys crocea-constitutively expressed, quickly up-regulated upon stimulation with trivalent bacterial vaccine677863Manually annotated by BRENDA team
J774A.1 cellMus musculus--717466Manually annotated by BRENDA team
kidneyOncorhynchus mykiss--171041Manually annotated by BRENDA team
kidneyRattus norvegicus--171067Manually annotated by BRENDA team
kidneyBos taurusP80189-171093Manually annotated by BRENDA team
kidneyOvis ariesP80190-171093Manually annotated by BRENDA team
kidneyOryctolagus cuniculus--171108Manually annotated by BRENDA team
kidneyLarimichthys crocea-constitutively expressed, quickly up-regulated upon stimulation with trivalent bacterial vaccine677863Manually annotated by BRENDA team
larvaMusca domestica--171102Manually annotated by BRENDA team
larvaHelicoverpa zea-salivary gland. Expression is not detected on day 0 of the fifth-instar, but reaches the highest level on day 1 and decreases thereafter. mRNA level is the highest from larva fed on tomato, followed by cotton and tobacco, with larvae fed on artificial diet being the lowest665818Manually annotated by BRENDA team
larvaMusca domestica-midgut681655Manually annotated by BRENDA team
latexCarica papaya--171080Manually annotated by BRENDA team
latexFicus sp.--171086Manually annotated by BRENDA team
liverRattus norvegicus--171054Manually annotated by BRENDA team
liverLarimichthys crocea-constitutively expressed677863Manually annotated by BRENDA team
macrophageOryctolagus cuniculus-alveolar171055Manually annotated by BRENDA team
macrophageMus musculus--717466Manually annotated by BRENDA team
malpighian tubuleAnopheles gambiaeA4ZWD2, Q7QHB9of adult female698287Manually annotated by BRENDA team
midgutAnopheles stephensi-activity reaches highest level in 4-8 days old mosquitoes680112Manually annotated by BRENDA team
midgutMusca domestica-from larva681655Manually annotated by BRENDA team
midgutAnopheles gambiaeA4ZWD2, Q7QHB9blood feeding results in significantly increased transcript abundance; blood feeding results in significantly increased transcript abundance698287Manually annotated by BRENDA team
midgutMusca domesticaB3GQR5high protein expression699304Manually annotated by BRENDA team
midgutRhodnius prolixusA9LN31, A9LN32predominant expression after ingestion of Trypanosoma cruzi in a bloodmeal, or after injection of bacteria699392Manually annotated by BRENDA team
midgut glandSaxidomus purpuratus--679932Manually annotated by BRENDA team
milkHomo sapiens--171036, 171047, 171075, 171088, 679303, 681099, 718276Manually annotated by BRENDA team
milkEquus caballus--171074, 171091, 682754, 710467Manually annotated by BRENDA team
milkPapio cynocephalus--171078Manually annotated by BRENDA team
milkCanis lupus familiaris--171098, 701125Manually annotated by BRENDA team
milkCanis lupus familiaris-equilibrium and kinetics of the folding and unfolding of lysozyme678277Manually annotated by BRENDA team
pancreatic juiceHomo sapiens--171047Manually annotated by BRENDA team
rennetBos taurus--171049Manually annotated by BRENDA team
rootMedicago sativa--171096Manually annotated by BRENDA team
salivaHomo sapiens-parotid171085Manually annotated by BRENDA team
salivaHomo sapiens--677858Manually annotated by BRENDA team
salivary glandHelicoverpa zea-of larva. Expression is not detected on day 0 of the fifth-instar, but reaches the highest level on day 1 and decreases thereafter. mRNA level is the highest from larva fed on tomato, followed by cotton and tobacco, with larvae fed on artificial diet being the lowest665818Manually annotated by BRENDA team
salivary glandAnopheles stephensi-activity reaches highest level in 4-8 days old mosquitoes680112Manually annotated by BRENDA team
serumHomo sapiens--171066Manually annotated by BRENDA team
serumCanis lupus familiaris--171071Manually annotated by BRENDA team
skin exudateBufo andrewsi--664671Manually annotated by BRENDA team
spleenLarimichthys crocea-constitutively expressed, quickly up-regulated upon stimulation with trivalent bacterial vaccine677863Manually annotated by BRENDA team
stomachRuminantia-fundic region highest activity171045Manually annotated by BRENDA team
stomachBos taurusQ06283-697903Manually annotated by BRENDA team
tearHomo sapiens--171066, 718120Manually annotated by BRENDA team
testisHomo sapiensQ86SG7-718120Manually annotated by BRENDA team
U-937 cellHomo sapiens--171034Manually annotated by BRENDA team
urineHomo sapiens-leukemia patients171066, 171084Manually annotated by BRENDA team
milkBos taurus--679303Manually annotated by BRENDA team
additional informationGallus gallus-two serine-rich heptapeptides, Ser-Ser-Ser-Lys-Ser-Ser-Ser (S6K) and Ser-Ser-Ser-Ser-Ser-Ser-Ser (S7) are fused to the C-terminus of chicken lysozyme by genetic modification. The cDNAs of S6K-lysozyme and S7-lysozyme are inserted into the expression vector of Pichia pastoris and secreted in the yeast cultivation medium. The secretion amounts of S6K-lysozyme and S7-lysozyme are about 60% of that of wild-type lysozyme664351Manually annotated by BRENDA team
additional informationHelicoverpa armigeraQ19R28gene expression is transiently enhanced at the onset of metamorphosis. Expression is up-regulated after the injection of Escherichia coli or entomopathogenic fungi, but shows different expression patterns695906Manually annotated by BRENDA team
additional informationMusca domesticaB3GQR5low expression at embryo stage. MRNA is upregulated 2 h post bacterial challenge, maintained for 6 h, and slightly declines from 12 to 24 h post-injection699304Manually annotated by BRENDA team

LOCALIZATION ORGANISM UNIPROT ACCESSION NO. COMMENTARY GeneOntology No. LITERATURE SOURCE
extracellularClostridium acetobutylicum---171101Manually annotated by BRENDA team
extracellularGallus gallus---717301, 718309Manually annotated by BRENDA team
extracellularHomo sapiens---718120, 718276Manually annotated by BRENDA team
microsomeRattus norvegicus---171054Manually annotated by BRENDA team
mitochondrionRattus norvegicus--5739171054Manually annotated by BRENDA team
nucleusRattus norvegicus--5634171054, 171067Manually annotated by BRENDA team

PDBSCOPCATHORGANISM
153l, downloadSCOP (153l)CATH (153l)Anser anser anser
154l, downloadSCOP (154l)CATH (154l)Anser anser anser
1iiz, downloadSCOP (1iiz)CATH (1iiz)Antheraea mylitta
2wag, downloadSCOP (2wag)CATH (2wag)Bacillus anthracis
1gd6, downloadSCOP (1gd6)CATH (1gd6)Bombyx mori
2z2f, downloadSCOP (2z2f)CATH (2z2f)Bos taurus
1el1, downloadSCOP (1el1)CATH (1el1)Canis familiaris
1i56, downloadSCOP (1i56)CATH (1i56)Canis familiaris
1qqy, downloadSCOP (1qqy)CATH (1qqy)Canis familiaris
2cwi, downloadSCOP (2cwi)CATH (2cwi)Canis familiaris
2z2e, downloadSCOP (2z2e)CATH (2z2e)Canis familiaris
1dkj, downloadSCOP (1dkj)CATH (1dkj)Colinus virginianus
1dkk, downloadSCOP (1dkk)CATH (1dkk)Colinus virginianus
1mii, downloadSCOP (1mii)CATH (1mii)Conus magus
2ihl, downloadSCOP (2ihl)CATH (2ihl)Coturnix coturnix japonica
1gbs, downloadSCOP (1gbs)CATH (1gbs)Cygnus atratus
1lsp, downloadSCOP (1lsp)CATH (1lsp)Cygnus atratus
1am7, downloadSCOP (1am7)CATH (1am7)Enterobacteria phage lambda
1d9u, downloadSCOP (1d9u)CATH (1d9u)Enterobacteria phage lambda
3d3d, downloadSCOP (3d3d)CATH (3d3d)Enterobacteria phage lambda
1xjt, downloadSCOP (1xjt)CATH (1xjt)Enterobacteria phage P1
1xju, downloadSCOP (1xju)CATH (1xju)Enterobacteria phage P1
3hde, downloadSCOP (3hde)CATH (3hde)Enterobacteria phage P21
3hdf, downloadSCOP (3hdf)CATH (3hdf)Enterobacteria phage P21
2anv, downloadSCOP (2anv)CATH (2anv)Enterobacteria phage P22
2anx, downloadSCOP (2anx)CATH (2anx)Enterobacteria phage P22
107l, downloadSCOP (107l)CATH (107l)Enterobacteria phage T4
108l, downloadSCOP (108l)CATH (108l)Enterobacteria phage T4
109l, downloadSCOP (109l)CATH (109l)Enterobacteria phage T4
110l, downloadSCOP (110l)CATH (110l)Enterobacteria phage T4
111l, downloadSCOP (111l)CATH (111l)Enterobacteria phage T4
112l, downloadSCOP (112l)CATH (112l)Enterobacteria phage T4
113l, downloadSCOP (113l)CATH (113l)Enterobacteria phage T4
114l, downloadSCOP (114l)CATH (114l)Enterobacteria phage T4
115l, downloadSCOP (115l)CATH (115l)Enterobacteria phage T4
118l, downloadSCOP (118l)CATH (118l)Enterobacteria phage T4
119l, downloadSCOP (119l)CATH (119l)Enterobacteria phage T4
120l, downloadSCOP (120l)CATH (120l)Enterobacteria phage T4
122l, downloadSCOP (122l)CATH (122l)Enterobacteria phage T4
123l, downloadSCOP (123l)CATH (123l)Enterobacteria phage T4
125l, downloadSCOP (125l)CATH (125l)Enterobacteria phage T4
126l, downloadSCOP (126l)CATH (126l)Enterobacteria phage T4
127l, downloadSCOP (127l)CATH (127l)Enterobacteria phage T4
128l, downloadSCOP (128l)CATH (128l)Enterobacteria phage T4
129l, downloadSCOP (129l)CATH (129l)Enterobacteria phage T4
130l, downloadSCOP (130l)CATH (130l)Enterobacteria phage T4
131l, downloadSCOP (131l)CATH (131l)Enterobacteria phage T4
137l, downloadSCOP (137l)CATH (137l)Enterobacteria phage T4
138l, downloadSCOP (138l)CATH (138l)Enterobacteria phage T4
139l, downloadSCOP (139l)CATH (139l)Enterobacteria phage T4
140l, downloadSCOP (140l)CATH (140l)Enterobacteria phage T4
141l, downloadSCOP (141l)CATH (141l)Enterobacteria phage T4
142l, downloadSCOP (142l)CATH (142l)Enterobacteria phage T4
143l, downloadSCOP (143l)CATH (143l)Enterobacteria phage T4
144l, downloadSCOP (144l)CATH (144l)Enterobacteria phage T4
145l, downloadSCOP (145l)CATH (145l)Enterobacteria phage T4
146l, downloadSCOP (146l)CATH (146l)Enterobacteria phage T4
147l, downloadSCOP (147l)CATH (147l)Enterobacteria phage T4
148l, downloadSCOP (148l)CATH (148l)Enterobacteria phage T4
149l, downloadSCOP (149l)CATH (149l)Enterobacteria phage T4
150l, downloadSCOP (150l)CATH (150l)Enterobacteria phage T4
151l, downloadSCOP (151l)CATH (151l)Enterobacteria phage T4
152l, downloadSCOP (152l)CATH (152l)Enterobacteria phage T4
155l, downloadSCOP (155l)CATH (155l)Enterobacteria phage T4
156l, downloadSCOP (156l)CATH (156l)Enterobacteria phage T4
157l, downloadSCOP (157l)CATH (157l)Enterobacteria phage T4
158l, downloadSCOP (158l)CATH (158l)Enterobacteria phage T4
159l, downloadSCOP (159l)CATH (159l)Enterobacteria phage T4
160l, downloadSCOP (160l)CATH (160l)Enterobacteria phage T4
161l, downloadSCOP (161l)CATH (161l)Enterobacteria phage T4
162l, downloadSCOP (162l)CATH (162l)Enterobacteria phage T4
163l, downloadSCOP (163l)CATH (163l)Enterobacteria phage T4
164l, downloadSCOP (164l)CATH (164l)Enterobacteria phage T4
165l, downloadSCOP (165l)CATH (165l)Enterobacteria phage T4
166l, downloadSCOP (166l)CATH (166l)Enterobacteria phage T4
167l, downloadSCOP (167l)CATH (167l)Enterobacteria phage T4
168l, downloadSCOP (168l)CATH (168l)Enterobacteria phage T4
169l, downloadSCOP (169l)CATH (169l)Enterobacteria phage T4
170l, downloadSCOP (170l)CATH (170l)Enterobacteria phage T4
171l, downloadSCOP (171l)CATH (171l)Enterobacteria phage T4
172l, downloadSCOP (172l)CATH (172l)Enterobacteria phage T4
173l, downloadSCOP (173l)CATH (173l)Enterobacteria phage T4
174l, downloadSCOP (174l)CATH (174l)Enterobacteria phage T4
175l, downloadSCOP (175l)CATH (175l)Enterobacteria phage T4
176l, downloadSCOP (176l)CATH (176l)Enterobacteria phage T4
177l, downloadSCOP (177l)CATH (177l)Enterobacteria phage T4
178l, downloadSCOP (178l)CATH (178l)Enterobacteria phage T4
180l, downloadSCOP (180l)CATH (180l)Enterobacteria phage T4
181l, downloadSCOP (181l)CATH (181l)Enterobacteria phage T4
182l, downloadSCOP (182l)CATH (182l)Enterobacteria phage T4
183l, downloadSCOP (183l)CATH (183l)Enterobacteria phage T4
184l, downloadSCOP (184l)CATH (184l)Enterobacteria phage T4
185l, downloadSCOP (185l)CATH (185l)Enterobacteria phage T4
186l, downloadSCOP (186l)CATH (186l)Enterobacteria phage T4
187l, downloadSCOP (187l)CATH (187l)Enterobacteria phage T4
188l, downloadSCOP (188l)CATH (188l)Enterobacteria phage T4
189l, downloadSCOP (189l)CATH (189l)Enterobacteria phage T4
190l, downloadSCOP (190l)CATH (190l)Enterobacteria phage T4
191l, downloadSCOP (191l)CATH (191l)Enterobacteria phage T4
192l, downloadSCOP (192l)CATH (192l)Enterobacteria phage T4
195l, downloadSCOP (195l)CATH (195l)Enterobacteria phage T4
196l, downloadSCOP (196l)CATH (196l)Enterobacteria phage T4
197l, downloadSCOP (197l)CATH (197l)Enterobacteria phage T4
198l, downloadSCOP (198l)CATH (198l)Enterobacteria phage T4
199l, downloadSCOP (199l)CATH (199l)Enterobacteria phage T4
1b6i, downloadSCOP (1b6i)CATH (1b6i)Enterobacteria phage T4
1c60, downloadSCOP (1c60)CATH (1c60)Enterobacteria phage T4
1c61, downloadSCOP (1c61)CATH (1c61)Enterobacteria phage T4
1c62, downloadSCOP (1c62)CATH (1c62)Enterobacteria phage T4
1c63, downloadSCOP (1c63)CATH (1c63)Enterobacteria phage T4
1c64, downloadSCOP (1c64)CATH (1c64)Enterobacteria phage T4
1c65, downloadSCOP (1c65)CATH (1c65)Enterobacteria phage T4
1c66, downloadSCOP (1c66)CATH (1c66)Enterobacteria phage T4
1c67, downloadSCOP (1c67)CATH (1c67)Enterobacteria phage T4
1c68, downloadSCOP (1c68)CATH (1c68)Enterobacteria phage T4
1c69, downloadSCOP (1c69)CATH (1c69)Enterobacteria phage T4
1c6a, downloadSCOP (1c6a)CATH (1c6a)Enterobacteria phage T4
1c6b, downloadSCOP (1c6b)CATH (1c6b)Enterobacteria phage T4
1c6c, downloadSCOP (1c6c)CATH (1c6c)Enterobacteria phage T4
1c6d, downloadSCOP (1c6d)CATH (1c6d)Enterobacteria phage T4
1c6e, downloadSCOP (1c6e)CATH (1c6e)Enterobacteria phage T4
1c6f, downloadSCOP (1c6f)CATH (1c6f)Enterobacteria phage T4
1c6g, downloadSCOP (1c6g)CATH (1c6g)Enterobacteria phage T4
1c6h, downloadSCOP (1c6h)CATH (1c6h)Enterobacteria phage T4
1c6i, downloadSCOP (1c6i)CATH (1c6i)Enterobacteria phage T4
1c6j, downloadSCOP (1c6j)CATH (1c6j)Enterobacteria phage T4
1c6k, downloadSCOP (1c6k)CATH (1c6k)Enterobacteria phage T4
1c6l, downloadSCOP (1c6l)CATH (1c6l)Enterobacteria phage T4
1c6m, downloadSCOP (1c6m)CATH (1c6m)Enterobacteria phage T4
1c6n, downloadSCOP (1c6n)CATH (1c6n)Enterobacteria phage T4
1c6p, downloadSCOP (1c6p)CATH (1c6p)Enterobacteria phage T4
1c6q, downloadSCOP (1c6q)CATH (1c6q)Enterobacteria phage T4
1c6t, downloadSCOP (1c6t)CATH (1c6t)Enterobacteria phage T4
1ctw, downloadSCOP (1ctw)CATH (1ctw)Enterobacteria phage T4
1cu0, downloadSCOP (1cu0)CATH (1cu0)Enterobacteria phage T4
1cu2, downloadSCOP (1cu2)CATH (1cu2)Enterobacteria phage T4
1cu3, downloadSCOP (1cu3)CATH (1cu3)Enterobacteria phage T4
1cu5, downloadSCOP (1cu5)CATH (1cu5)Enterobacteria phage T4
1cu6, downloadSCOP (1cu6)CATH (1cu6)Enterobacteria phage T4
1cup, downloadSCOP (1cup)CATH (1cup)Enterobacteria phage T4
1cuq, downloadSCOP (1cuq)CATH (1cuq)Enterobacteria phage T4
1cv0, downloadSCOP (1cv0)CATH (1cv0)Enterobacteria phage T4
1cv1, downloadSCOP (1cv1)CATH (1cv1)Enterobacteria phage T4
1cv3, downloadSCOP (1cv3)CATH (1cv3)Enterobacteria phage T4
1cv4, downloadSCOP (1cv4)CATH (1cv4)Enterobacteria phage T4
1cv5, downloadSCOP (1cv5)CATH (1cv5)Enterobacteria phage T4
1cv6, downloadSCOP (1cv6)CATH (1cv6)Enterobacteria phage T4
1cvk, downloadSCOP (1cvk)CATH (1cvk)Enterobacteria phage T4
1cx6, downloadSCOP (1cx6)CATH (1cx6)Enterobacteria phage T4
1cx7, downloadSCOP (1cx7)CATH (1cx7)Enterobacteria phage T4
1d2w, downloadSCOP (1d2w)CATH (1d2w)Enterobacteria phage T4
1d2y, downloadSCOP (1d2y)CATH (1d2y)Enterobacteria phage T4
1d3f, downloadSCOP (1d3f)CATH (1d3f)Enterobacteria phage T4
1d3j, downloadSCOP (1d3j)CATH (1d3j)Enterobacteria phage T4
1d3m, downloadSCOP (1d3m)CATH (1d3m)Enterobacteria phage T4
1d3n, downloadSCOP (1d3n)CATH (1d3n)Enterobacteria phage T4
1d9w, downloadSCOP (1d9w)CATH (1d9w)Enterobacteria phage T4
1dya, downloadSCOP (1dya)CATH (1dya)Enterobacteria phage T4
1dyb, downloadSCOP (1dyb)CATH (1dyb)Enterobacteria phage T4
1dyc, downloadSCOP (1dyc)CATH (1dyc)Enterobacteria phage T4
1dyd, downloadSCOP (1dyd)CATH (1dyd)Enterobacteria phage T4
1dye, downloadSCOP (1dye)CATH (1dye)Enterobacteria phage T4
1dyf, downloadSCOP (1dyf)CATH (1dyf)Enterobacteria phage T4
1dyg, downloadSCOP (1dyg)CATH (1dyg)Enterobacteria phage T4
1epy, downloadSCOP (1epy)CATH (1epy)Enterobacteria phage T4
1g06, downloadSCOP (1g06)CATH (1g06)Enterobacteria phage T4
1g07, downloadSCOP (1g07)CATH (1g07)Enterobacteria phage T4
1g0g, downloadSCOP (1g0g)CATH (1g0g)Enterobacteria phage T4
1g0j, downloadSCOP (1g0j)CATH (1g0j)Enterobacteria phage T4
1g0k, downloadSCOP (1g0k)CATH (1g0k)Enterobacteria phage T4
1g0l, downloadSCOP (1g0l)CATH (1g0l)Enterobacteria phage T4
1g0m, downloadSCOP (1g0m)CATH (1g0m)Enterobacteria phage T4
1g0p, downloadSCOP (1g0p)CATH (1g0p)Enterobacteria phage T4
1g0q, downloadSCOP (1g0q)CATH (1g0q)Enterobacteria phage T4
1g1v, downloadSCOP (1g1v)CATH (1g1v)Enterobacteria phage T4
1g1w, downloadSCOP (1g1w)CATH (1g1w)Enterobacteria phage T4
1i6s, downloadSCOP (1i6s)CATH (1i6s)Enterobacteria phage T4
1jqu, downloadSCOP (1jqu)CATH (1jqu)Enterobacteria phage T4
1jtm, downloadSCOP (1jtm)CATH (1jtm)Enterobacteria phage T4
1jtn, downloadSCOP (1jtn)CATH (1jtn)Enterobacteria phage T4
1k28, downloadSCOP (1k28)CATH (1k28)Enterobacteria phage T4
1kni, downloadSCOP (1kni)CATH (1kni)Enterobacteria phage T4
1ks3, downloadSCOP (1ks3)CATH (1ks3)Enterobacteria phage T4
1kw5, downloadSCOP (1kw5)CATH (1kw5)Enterobacteria phage T4
1kw7, downloadSCOP (1kw7)CATH (1kw7)Enterobacteria phage T4
1ky0, downloadSCOP (1ky0)CATH (1ky0)Enterobacteria phage T4
1ky1, downloadSCOP (1ky1)CATH (1ky1)Enterobacteria phage T4
1l00, downloadSCOP (1l00)CATH (1l00)Enterobacteria phage T4
1l01, downloadSCOP (1l01)CATH (1l01)Enterobacteria phage T4
1l02, downloadSCOP (1l02)CATH (1l02)Enterobacteria phage T4
1l03, downloadSCOP (1l03)CATH (1l03)Enterobacteria phage T4
1l04, downloadSCOP (1l04)CATH (1l04)Enterobacteria phage T4
1l05, downloadSCOP (1l05)CATH (1l05)Enterobacteria phage T4
1l06, downloadSCOP (1l06)CATH (1l06)Enterobacteria phage T4
1l07, downloadSCOP (1l07)CATH (1l07)Enterobacteria phage T4
1l08, downloadSCOP (1l08)CATH (1l08)Enterobacteria phage T4
1l09, downloadSCOP (1l09)CATH (1l09)Enterobacteria phage T4
1l0j, downloadSCOP (1l0j)CATH (1l0j)Enterobacteria phage T4
1l0k, downloadSCOP (1l0k)CATH (1l0k)Enterobacteria phage T4
1l10, downloadSCOP (1l10)CATH (1l10)Enterobacteria phage T4
1l11, downloadSCOP (1l11)CATH (1l11)Enterobacteria phage T4
1l12, downloadSCOP (1l12)CATH (1l12)Enterobacteria phage T4
1l13, downloadSCOP (1l13)CATH (1l13)Enterobacteria phage T4
1l14, downloadSCOP (1l14)CATH (1l14)Enterobacteria phage T4
1l15, downloadSCOP (1l15)CATH (1l15)Enterobacteria phage T4
1l16, downloadSCOP (1l16)CATH (1l16)Enterobacteria phage T4
1l17, downloadSCOP (1l17)CATH (1l17)Enterobacteria phage T4
1l18, downloadSCOP (1l18)CATH (1l18)Enterobacteria phage T4
1l19, downloadSCOP (1l19)CATH (1l19)Enterobacteria phage T4
1l20, downloadSCOP (1l20)CATH (1l20)Enterobacteria phage T4
1l21, downloadSCOP (1l21)CATH (1l21)Enterobacteria phage T4
1l22, downloadSCOP (1l22)CATH (1l22)Enterobacteria phage T4
1l23, downloadSCOP (1l23)CATH (1l23)Enterobacteria phage T4
1l24, downloadSCOP (1l24)CATH (1l24)Enterobacteria phage T4
1l25, downloadSCOP (1l25)CATH (1l25)Enterobacteria phage T4
1l26, downloadSCOP (1l26)CATH (1l26)Enterobacteria phage T4
1l27, downloadSCOP (1l27)CATH (1l27)Enterobacteria phage T4
1l28, downloadSCOP (1l28)CATH (1l28)Enterobacteria phage T4
1l29, downloadSCOP (1l29)CATH (1l29)Enterobacteria phage T4
1l30, downloadSCOP (1l30)CATH (1l30)Enterobacteria phage T4
1l31, downloadSCOP (1l31)CATH (1l31)Enterobacteria phage T4
1l32, downloadSCOP (1l32)CATH (1l32)Enterobacteria phage T4
1l33, downloadSCOP (1l33)CATH (1l33)Enterobacteria phage T4
1l34, downloadSCOP (1l34)CATH (1l34)Enterobacteria phage T4
1l35, downloadSCOP (1l35)CATH (1l35)Enterobacteria phage T4
1l36, downloadSCOP (1l36)CATH (1l36)Enterobacteria phage T4
1l37, downloadSCOP (1l37)CATH (1l37)Enterobacteria phage T4
1l38, downloadSCOP (1l38)CATH (1l38)Enterobacteria phage T4
1l39, downloadSCOP (1l39)CATH (1l39)Enterobacteria phage T4
1l40, downloadSCOP (1l40)CATH (1l40)Enterobacteria phage T4
1l41, downloadSCOP (1l41)CATH (1l41)Enterobacteria phage T4
1l42, downloadSCOP (1l42)CATH (1l42)Enterobacteria phage T4
1l43, downloadSCOP (1l43)CATH (1l43)Enterobacteria phage T4
1l44, downloadSCOP (1l44)CATH (1l44)Enterobacteria phage T4
1l45, downloadSCOP (1l45)CATH (1l45)Enterobacteria phage T4
1l46, downloadSCOP (1l46)CATH (1l46)Enterobacteria phage T4
1l47, downloadSCOP (1l47)CATH (1l47)Enterobacteria phage T4
1l48, downloadSCOP (1l48)CATH (1l48)Enterobacteria phage T4
1l49, downloadSCOP (1l49)CATH (1l49)Enterobacteria phage T4
1l50, downloadSCOP (1l50)CATH (1l50)Enterobacteria phage T4
1l51, downloadSCOP (1l51)CATH (1l51)Enterobacteria phage T4
1l52, downloadSCOP (1l52)CATH (1l52)Enterobacteria phage T4
1l53, downloadSCOP (1l53)CATH (1l53)Enterobacteria phage T4
1l54, downloadSCOP (1l54)CATH (1l54)Enterobacteria phage T4
1l55, downloadSCOP (1l55)CATH (1l55)Enterobacteria phage T4
1l56, downloadSCOP (1l56)CATH (1l56)Enterobacteria phage T4
1l57, downloadSCOP (1l57)CATH (1l57)Enterobacteria phage T4
1l58, downloadSCOP (1l58)CATH (1l58)Enterobacteria phage T4
1l59, downloadSCOP (1l59)CATH (1l59)Enterobacteria phage T4
1l60, downloadSCOP (1l60)CATH (1l60)Enterobacteria phage T4
1l61, downloadSCOP (1l61)CATH (1l61)Enterobacteria phage T4
1l62, downloadSCOP (1l62)CATH (1l62)Enterobacteria phage T4
1l63, downloadSCOP (1l63)CATH (1l63)Enterobacteria phage T4
1l64, downloadSCOP (1l64)CATH (1l64)Enterobacteria phage T4
1l65, downloadSCOP (1l65)CATH (1l65)Enterobacteria phage T4
1l66, downloadSCOP (1l66)CATH (1l66)Enterobacteria phage T4
1l67, downloadSCOP (1l67)CATH (1l67)Enterobacteria phage T4
1l68, downloadSCOP (1l68)CATH (1l68)Enterobacteria phage T4
1l69, downloadSCOP (1l69)CATH (1l69)Enterobacteria phage T4
1l70, downloadSCOP (1l70)CATH (1l70)Enterobacteria phage T4
1l71, downloadSCOP (1l71)CATH (1l71)Enterobacteria phage T4
1l72, downloadSCOP (1l72)CATH (1l72)Enterobacteria phage T4
1l73, downloadSCOP (1l73)CATH (1l73)Enterobacteria phage T4
1l74, downloadSCOP (1l74)CATH (1l74)Enterobacteria phage T4
1l75, downloadSCOP (1l75)CATH (1l75)Enterobacteria phage T4
1l76, downloadSCOP (1l76)CATH (1l76)Enterobacteria phage T4
1l77, downloadSCOP (1l77)CATH (1l77)Enterobacteria phage T4
1l79, downloadSCOP (1l79)CATH (1l79)Enterobacteria phage T4
1l80, downloadSCOP (1l80)CATH (1l80)Enterobacteria phage T4
1l81, downloadSCOP (1l81)CATH (1l81)Enterobacteria phage T4
1l82, downloadSCOP (1l82)CATH (1l82)Enterobacteria phage T4
1l83, downloadSCOP (1l83)CATH (1l83)Enterobacteria phage T4
1l84, downloadSCOP (1l84)CATH (1l84)Enterobacteria phage T4
1l85, downloadSCOP (1l85)CATH (1l85)Enterobacteria phage T4
1l86, downloadSCOP (1l86)CATH (1l86)Enterobacteria phage T4
1l87, downloadSCOP (1l87)CATH (1l87)Enterobacteria phage T4
1l88, downloadSCOP (1l88)CATH (1l88)Enterobacteria phage T4
1l89, downloadSCOP (1l89)CATH (1l89)Enterobacteria phage T4
1l90, downloadSCOP (1l90)CATH (1l90)Enterobacteria phage T4
1l91, downloadSCOP (1l91)CATH (1l91)Enterobacteria phage T4
1l92, downloadSCOP (1l92)CATH (1l92)Enterobacteria phage T4
1l93, downloadSCOP (1l93)CATH (1l93)Enterobacteria phage T4
1l94, downloadSCOP (1l94)CATH (1l94)Enterobacteria phage T4
1l95, downloadSCOP (1l95)CATH (1l95)Enterobacteria phage T4
1l96, downloadSCOP (1l96)CATH (1l96)Enterobacteria phage T4
1l97, downloadSCOP (1l97)CATH (1l97)Enterobacteria phage T4
1l98, downloadSCOP (1l98)CATH (1l98)Enterobacteria phage T4
1l99, downloadSCOP (1l99)CATH (1l99)Enterobacteria phage T4
1lgu, downloadSCOP (1lgu)CATH (1lgu)Enterobacteria phage T4
1lgw, downloadSCOP (1lgw)CATH (1lgw)Enterobacteria phage T4
1lgx, downloadSCOP (1lgx)CATH (1lgx)Enterobacteria phage T4
1li2, downloadSCOP (1li2)CATH (1li2)Enterobacteria phage T4
1li3, downloadSCOP (1li3)CATH (1li3)Enterobacteria phage T4
1li6, downloadSCOP (1li6)CATH (1li6)Enterobacteria phage T4
1llh, downloadSCOP (1llh)CATH (1llh)Enterobacteria phage T4
1lpy, downloadSCOP (1lpy)CATH (1lpy)Enterobacteria phage T4
1lw9, downloadSCOP (1lw9)CATH (1lw9)Enterobacteria phage T4
1lwg, downloadSCOP (1lwg)CATH (1lwg)Enterobacteria phage T4
1lwk, downloadSCOP (1lwk)CATH (1lwk)Enterobacteria phage T4
1nhb, downloadSCOP (1nhb)CATH (1nhb)Enterobacteria phage T4
1ov5, downloadSCOP (1ov5)CATH (1ov5)Enterobacteria phage T4
1ov7, downloadSCOP (1ov7)CATH (1ov7)Enterobacteria phage T4
1ovh, downloadSCOP (1ovh)CATH (1ovh)Enterobacteria phage T4
1ovj, downloadSCOP (1ovj)CATH (1ovj)Enterobacteria phage T4
1ovk, downloadSCOP (1ovk)CATH (1ovk)Enterobacteria phage T4
1owy, downloadSCOP (1owy)CATH (1owy)Enterobacteria phage T4
1owz, downloadSCOP (1owz)CATH (1owz)Enterobacteria phage T4
1oyu, downloadSCOP (1oyu)CATH (1oyu)Enterobacteria phage T4
1p2l, downloadSCOP (1p2l)CATH (1p2l)Enterobacteria phage T4
1p2r, downloadSCOP (1p2r)CATH (1p2r)Enterobacteria phage T4
1p36, downloadSCOP (1p36)CATH (1p36)Enterobacteria phage T4
1p37, downloadSCOP (1p37)CATH (1p37)Enterobacteria phage T4
1p3n, downloadSCOP (1p3n)CATH (1p3n)Enterobacteria phage T4
1p46, downloadSCOP (1p46)CATH (1p46)Enterobacteria phage T4
1p56, downloadSCOP (1p56)CATH (1p56)Enterobacteria phage T4
1p5c, downloadSCOP (1p5c)CATH (1p5c)Enterobacteria phage T4
1p64, downloadSCOP (1p64)CATH (1p64)Enterobacteria phage T4
1p6y, downloadSCOP (1p6y)CATH (1p6y)Enterobacteria phage T4
1p7s, downloadSCOP (1p7s)CATH (1p7s)Enterobacteria phage T4
1pdl, downloadSCOP (1pdl)CATH (1pdl)Enterobacteria phage T4
1pqd, downloadSCOP (1pqd)CATH (1pqd)Enterobacteria phage T4
1pqi, downloadSCOP (1pqi)CATH (1pqi)Enterobacteria phage T4
1pqj, downloadSCOP (1pqj)CATH (1pqj)Enterobacteria phage T4
1pqk, downloadSCOP (1pqk)CATH (1pqk)Enterobacteria phage T4
1pqm, downloadSCOP (1pqm)CATH (1pqm)Enterobacteria phage T4
1pqo, downloadSCOP (1pqo)CATH (1pqo)Enterobacteria phage T4
1qs5, downloadSCOP (1qs5)CATH (1qs5)Enterobacteria phage T4
1qs9, downloadSCOP (1qs9)CATH (1qs9)Enterobacteria phage T4
1qsb, downloadSCOP (1qsb)CATH (1qsb)Enterobacteria phage T4
1qsq, downloadSCOP (1qsq)CATH (1qsq)Enterobacteria phage T4
1qt3, downloadSCOP (1qt3)CATH (1qt3)Enterobacteria phage T4
1qt4, downloadSCOP (1qt4)CATH (1qt4)Enterobacteria phage T4
1qt5, downloadSCOP (1qt5)CATH (1qt5)Enterobacteria phage T4
1qt6, downloadSCOP (1qt6)CATH (1qt6)Enterobacteria phage T4
1qt7, downloadSCOP (1qt7)CATH (1qt7)Enterobacteria phage T4
1qt8, downloadSCOP (1qt8)CATH (1qt8)Enterobacteria phage T4
1qtb, downloadSCOP (1qtb)CATH (1qtb)Enterobacteria phage T4
1qtc, downloadSCOP (1qtc)CATH (1qtc)Enterobacteria phage T4
1qtd, downloadSCOP (1qtd)CATH (1qtd)Enterobacteria phage T4
1qth, downloadSCOP (1qth)CATH (1qth)Enterobacteria phage T4
1qtv, downloadSCOP (1qtv)CATH (1qtv)Enterobacteria phage T4
1qtz, downloadSCOP (1qtz)CATH (1qtz)Enterobacteria phage T4
1qud, downloadSCOP (1qud)CATH (1qud)Enterobacteria phage T4
1qug, downloadSCOP (1qug)CATH (1qug)Enterobacteria phage T4
1quh, downloadSCOP (1quh)CATH (1quh)Enterobacteria phage T4
1quo, downloadSCOP (1quo)CATH (1quo)Enterobacteria phage T4
1ssw, downloadSCOP (1ssw)CATH (1ssw)Enterobacteria phage T4
1ssy, downloadSCOP (1ssy)CATH (1ssy)Enterobacteria phage T4
1swy, downloadSCOP (1swy)CATH (1swy)Enterobacteria phage T4
1swz, downloadSCOP (1swz)CATH (1swz)Enterobacteria phage T4
1sx2, downloadSCOP (1sx2)CATH (1sx2)Enterobacteria phage T4
1sx7, downloadSCOP (1sx7)CATH (1sx7)Enterobacteria phage T4
1t6h, downloadSCOP (1t6h)CATH (1t6h)Enterobacteria phage T4
1t8a, downloadSCOP (1t8a)CATH (1t8a)Enterobacteria phage T4
1t8f, downloadSCOP (1t8f)CATH (1t8f)Enterobacteria phage T4
1t8g, downloadSCOP (1t8g)CATH (1t8g)Enterobacteria phage T4
1t97, downloadSCOP (1t97)CATH (1t97)Enterobacteria phage T4
1tla, downloadSCOP (1tla)CATH (1tla)Enterobacteria phage T4
1wth, downloadSCOP (1wth)CATH (1wth)Enterobacteria phage T4
1xep, downloadSCOP (1xep)CATH (1xep)Enterobacteria phage T4
1zur, downloadSCOP (1zur)CATH (1zur)Enterobacteria phage T4
1zwn, downloadSCOP (1zwn)CATH (1zwn)Enterobacteria phage T4
1zyt, downloadSCOP (1zyt)CATH (1zyt)Enterobacteria phage T4
200l, downloadSCOP (200l)CATH (200l)Enterobacteria phage T4
201l, downloadSCOP (201l)CATH (201l)Enterobacteria phage T4
205l, downloadSCOP (205l)CATH (205l)Enterobacteria phage T4
206l, downloadSCOP (206l)CATH (206l)Enterobacteria phage T4
209l, downloadSCOP (209l)CATH (209l)Enterobacteria phage T4
210l, downloadSCOP (210l)CATH (210l)Enterobacteria phage T4
211l, downloadSCOP (211l)CATH (211l)Enterobacteria phage T4
212l, downloadSCOP (212l)CATH (212l)Enterobacteria phage T4
213l, downloadSCOP (213l)CATH (213l)Enterobacteria phage T4
214l, downloadSCOP (214l)CATH (214l)Enterobacteria phage T4
215l, downloadSCOP (215l)CATH (215l)Enterobacteria phage T4
216l, downloadSCOP (216l)CATH (216l)Enterobacteria phage T4
217l, downloadSCOP (217l)CATH (217l)Enterobacteria phage T4
218l, downloadSCOP (218l)CATH (218l)Enterobacteria phage T4
219l, downloadSCOP (219l)CATH (219l)Enterobacteria phage T4
220l, downloadSCOP (220l)CATH (220l)Enterobacteria phage T4
221l, downloadSCOP (221l)CATH (221l)Enterobacteria phage T4
222l, downloadSCOP (222l)CATH (222l)Enterobacteria phage T4
223l, downloadSCOP (223l)CATH (223l)Enterobacteria phage T4
224l, downloadSCOP (224l)CATH (224l)Enterobacteria phage T4
225l, downloadSCOP (225l)CATH (225l)Enterobacteria phage T4
226l, downloadSCOP (226l)CATH (226l)Enterobacteria phage T4
227l, downloadSCOP (227l)CATH (227l)Enterobacteria phage T4
228l, downloadSCOP (228l)CATH (228l)Enterobacteria phage T4
229l, downloadSCOP (229l)CATH (229l)Enterobacteria phage T4
230l, downloadSCOP (230l)CATH (230l)Enterobacteria phage T4
231l, downloadSCOP (231l)CATH (231l)Enterobacteria phage T4
232l, downloadSCOP (232l)CATH (232l)Enterobacteria phage T4
233l, downloadSCOP (233l)CATH (233l)Enterobacteria phage T4
234l, downloadSCOP (234l)CATH (234l)Enterobacteria phage T4
235l, downloadSCOP (235l)CATH (235l)Enterobacteria phage T4
236l, downloadSCOP (236l)CATH (236l)Enterobacteria phage T4
237l, downloadSCOP (237l)CATH (237l)Enterobacteria phage T4
238l, downloadSCOP (238l)CATH (238l)Enterobacteria phage T4
239l, downloadSCOP (239l)CATH (239l)Enterobacteria phage T4
240l, downloadSCOP (240l)CATH (240l)Enterobacteria phage T4
241l, downloadSCOP (241l)CATH (241l)Enterobacteria phage T4
242l, downloadSCOP (242l)CATH (242l)Enterobacteria phage T4
243l, downloadSCOP (243l)CATH (243l)Enterobacteria phage T4
244l, downloadSCOP (244l)CATH (244l)Enterobacteria phage T4
245l, downloadSCOP (245l)CATH (245l)Enterobacteria phage T4
246l, downloadSCOP (246l)CATH (246l)Enterobacteria phage T4
247l, downloadSCOP (247l)CATH (247l)Enterobacteria phage T4
248l, downloadSCOP (248l)CATH (248l)Enterobacteria phage T4
249l, downloadSCOP (249l)CATH (249l)Enterobacteria phage T4
250l, downloadSCOP (250l)CATH (250l)Enterobacteria phage T4
251l, downloadSCOP (251l)CATH (251l)Enterobacteria phage T4
252l, downloadSCOP (252l)CATH (252l)Enterobacteria phage T4
253l, downloadSCOP (253l)CATH (253l)Enterobacteria phage T4
254l, downloadSCOP (254l)CATH (254l)Enterobacteria phage T4
255l, downloadSCOP (255l)CATH (255l)Enterobacteria phage T4
256l, downloadSCOP (256l)CATH (256l)Enterobacteria phage T4
257l, downloadSCOP (257l)CATH (257l)Enterobacteria phage T4
258l, downloadSCOP (258l)CATH (258l)Enterobacteria phage T4
259l, downloadSCOP (259l)CATH (259l)Enterobacteria phage T4
260l, downloadSCOP (260l)CATH (260l)Enterobacteria phage T4
261l, downloadSCOP (261l)CATH (261l)Enterobacteria phage T4
262l, downloadSCOP (262l)CATH (262l)Enterobacteria phage T4
2a4t, downloadSCOP (2a4t)CATH (2a4t)Enterobacteria phage T4
2b6t, downloadSCOP (2b6t)CATH (2b6t)Enterobacteria phage T4
2b6w, downloadSCOP (2b6w)CATH (2b6w)Enterobacteria phage T4
2b6x, downloadSCOP (2b6x)CATH (2b6x)Enterobacteria phage T4
2b6y, downloadSCOP (2b6y)CATH (2b6y)Enterobacteria phage T4
2b6z, downloadSCOP (2b6z)CATH (2b6z)Enterobacteria phage T4
2b70, downloadSCOP (2b70)CATH (2b70)Enterobacteria phage T4
2b72, downloadSCOP (2b72)CATH (2b72)Enterobacteria phage T4
2b73, downloadSCOP (2b73)CATH (2b73)Enterobacteria phage T4
2b74, downloadSCOP (2b74)CATH (2b74)Enterobacteria phage T4
2b75, downloadSCOP (2b75)CATH (2b75)Enterobacteria phage T4
2b7x, downloadSCOP (2b7x)CATH (2b7x)Enterobacteria phage T4
2cuu, downloadSCOP (2cuu)CATH (2cuu)Enterobacteria phage T4
2f2q, downloadSCOP (2f2q)CATH (2f2q)Enterobacteria phage T4
2f32, downloadSCOP (2f32)CATH (2f32)Enterobacteria phage T4
2f47, downloadSCOP (2f47)CATH (2f47)Enterobacteria phage T4
2huk, downloadSCOP (2huk)CATH (2huk)Enterobacteria phage T4
2hul, downloadSCOP (2hul)CATH (2hul)Enterobacteria phage T4
2hum, downloadSCOP (2hum)CATH (2hum)Enterobacteria phage T4
2igc, downloadSCOP (2igc)CATH (2igc)Enterobacteria phage T4
2l78, downloadSCOP (2l78)CATH (2l78)Enterobacteria phage T4
2lc9, downloadSCOP (2lc9)CATH (2lc9)Enterobacteria phage T4
2lcb, downloadSCOP (2lcb)CATH (2lcb)Enterobacteria phage T4
2lzm, downloadSCOP (2lzm)CATH (2lzm)Enterobacteria phage T4
2ntg, downloadSCOP (2ntg)CATH (2ntg)Enterobacteria phage T4
2nth, downloadSCOP (2nth)CATH (2nth)Enterobacteria phage T4
2o4w, downloadSCOP (2o4w)CATH (2o4w)Enterobacteria phage T4
2o79, downloadSCOP (2o79)CATH (2o79)Enterobacteria phage T4
2o7a, downloadSCOP (2o7a)CATH (2o7a)Enterobacteria phage T4
2oe4, downloadSCOP (2oe4)CATH (2oe4)Enterobacteria phage T4
2oe7, downloadSCOP (2oe7)CATH (2oe7)Enterobacteria phage T4
2oe9, downloadSCOP (2oe9)CATH (2oe9)Enterobacteria phage T4
2oea, downloadSCOP (2oea)CATH (2oea)Enterobacteria phage T4
2oty, downloadSCOP (2oty)CATH (2oty)Enterobacteria phage T4
2otz, downloadSCOP (2otz)CATH (2otz)Enterobacteria phage T4
2ou0, downloadSCOP (2ou0)CATH (2ou0)Enterobacteria phage T4
2ou8, downloadSCOP (2ou8)CATH (2ou8)Enterobacteria phage T4
2ou9, downloadSCOP (2ou9)CATH (2ou9)Enterobacteria phage T4
2q9d, downloadSCOP (2q9d)CATH (2q9d)Enterobacteria phage T4
2q9e, downloadSCOP (2q9e)CATH (2q9e)Enterobacteria phage T4
2qb0, downloadSCOP (2qb0)CATH (2qb0)Enterobacteria phage T4
2ray, downloadSCOP (2ray)CATH (2ray)Enterobacteria phage T4
2raz, downloadSCOP (2raz)CATH (2raz)Enterobacteria phage T4
2rb0, downloadSCOP (2rb0)CATH (2rb0)Enterobacteria phage T4
2rb1, downloadSCOP (2rb1)CATH (2rb1)Enterobacteria phage T4
2rb2, downloadSCOP (2rb2)CATH (2rb2)Enterobacteria phage T4
2rbn, downloadSCOP (2rbn)CATH (2rbn)Enterobacteria phage T4
2rbo, downloadSCOP (2rbo)CATH (2rbo)Enterobacteria phage T4
2rbp, downloadSCOP (2rbp)CATH (2rbp)Enterobacteria phage T4
2rbq, downloadSCOP (2rbq)CATH (2rbq)Enterobacteria phage T4
2rbr, downloadSCOP (2rbr)CATH (2rbr)Enterobacteria phage T4
2rbs, downloadSCOP (2rbs)CATH (2rbs)Enterobacteria phage T4
2z6b, downloadSCOP (2z6b)CATH (2z6b)Enterobacteria phage T4
3a1m, downloadSCOP (3a1m)CATH (3a1m)Enterobacteria phage T4
3c7w, downloadSCOP (3c7w)CATH (3c7w)Enterobacteria phage T4
3c7y, downloadSCOP (3c7y)CATH (3c7y)Enterobacteria phage T4
3c7z, downloadSCOP (3c7z)CATH (3c7z)Enterobacteria phage T4
3c80, downloadSCOP (3c80)CATH (3c80)Enterobacteria phage T4
3c81, downloadSCOP (3c81)CATH (3c81)Enterobacteria phage T4
3c82, downloadSCOP (3c82)CATH (3c82)Enterobacteria phage T4
3c83, downloadSCOP (3c83)CATH (3c83)Enterobacteria phage T4
3c8q, downloadSCOP (3c8q)CATH (3c8q)Enterobacteria phage T4
3c8r, downloadSCOP (3c8r)CATH (3c8r)Enterobacteria phage T4
3c8s, downloadSCOP (3c8s)CATH (3c8s)Enterobacteria phage T4
3cdo, downloadSCOP (3cdo)CATH (3cdo)Enterobacteria phage T4
3cdq, downloadSCOP (3cdq)CATH (3cdq)Enterobacteria phage T4
3cdr, downloadSCOP (3cdr)CATH (3cdr)Enterobacteria phage T4
3cdt, downloadSCOP (3cdt)CATH (3cdt)Enterobacteria phage T4
3cdv, downloadSCOP (3cdv)CATH (3cdv)Enterobacteria phage T4
3dke, downloadSCOP (3dke)CATH (3dke)Enterobacteria phage T4
3dmv, downloadSCOP (3dmv)CATH (3dmv)Enterobacteria phage T4
3dmx, downloadSCOP (3dmx)CATH (3dmx)Enterobacteria phage T4
3dmz, downloadSCOP (3dmz)CATH (3dmz)Enterobacteria phage T4
3dn0, downloadSCOP (3dn0)CATH (3dn0)Enterobacteria phage T4
3dn1, downloadSCOP (3dn1)CATH (3dn1)Enterobacteria phage T4
3dn2, downloadSCOP (3dn2)CATH (3dn2)Enterobacteria phage T4
3dn3, downloadSCOP (3dn3)CATH (3dn3)Enterobacteria phage T4
3dn4, downloadSCOP (3dn4)CATH (3dn4)Enterobacteria phage T4
3dn6, downloadSCOP (3dn6)CATH (3dn6)Enterobacteria phage T4
3dn8, downloadSCOP (3dn8)CATH (3dn8)Enterobacteria phage T4
3dna, downloadSCOP (3dna)CATH (3dna)Enterobacteria phage T4
3f8v, downloadSCOP (3f8v)CATH (3f8v)Enterobacteria phage T4
3f9l, downloadSCOP (3f9l)CATH (3f9l)Enterobacteria phage T4
3fa0, downloadSCOP (3fa0)CATH (3fa0)Enterobacteria phage T4
3fad, downloadSCOP (3fad)CATH (3fad)Enterobacteria phage T4
3fi5, downloadSCOP (3fi5)CATH (3fi5)Enterobacteria phage T4
3g3v, downloadSCOP (3g3v)CATH (3g3v)Enterobacteria phage T4
3g3w, downloadSCOP (3g3w)CATH (3g3w)Enterobacteria phage T4
3g3x, downloadSCOP (3g3x)CATH (3g3x)Enterobacteria phage T4
3gui, downloadSCOP (3gui)CATH (3gui)Enterobacteria phage T4
3guj, downloadSCOP (3guj)CATH (3guj)Enterobacteria phage T4
3guk, downloadSCOP (3guk)CATH (3guk)Enterobacteria phage T4
3gul, downloadSCOP (3gul)CATH (3gul)Enterobacteria phage T4
3gum, downloadSCOP (3gum)CATH (3gum)Enterobacteria phage T4
3gun, downloadSCOP (3gun)CATH (3gun)Enterobacteria phage T4
3guo, downloadSCOP (3guo)CATH (3guo)Enterobacteria phage T4
3gup, downloadSCOP (3gup)CATH (3gup)Enterobacteria phage T4
3hh3, downloadSCOP (3hh3)CATH (3hh3)Enterobacteria phage T4
3hh4, downloadSCOP (3hh4)CATH (3hh4)Enterobacteria phage T4
3hh5, downloadSCOP (3hh5)CATH (3hh5)Enterobacteria phage T4
3hh6, downloadSCOP (3hh6)CATH (3hh6)Enterobacteria phage T4
3ht6, downloadSCOP (3ht6)CATH (3ht6)Enterobacteria phage T4
3ht7, downloadSCOP (3ht7)CATH (3ht7)Enterobacteria phage T4
3ht8, downloadSCOP (3ht8)CATH (3ht8)Enterobacteria phage T4
3ht9, downloadSCOP (3ht9)CATH (3ht9)Enterobacteria phage T4
3htb, downloadSCOP (3htb)CATH (3htb)Enterobacteria phage T4
3htd, downloadSCOP (3htd)CATH (3htd)Enterobacteria phage T4
3htf, downloadSCOP (3htf)CATH (3htf)Enterobacteria phage T4
3htg, downloadSCOP (3htg)CATH (3htg)Enterobacteria phage T4
3hu8, downloadSCOP (3hu8)CATH (3hu8)Enterobacteria phage T4
3hu9, downloadSCOP (3hu9)CATH (3hu9)Enterobacteria phage T4
3hua, downloadSCOP (3hua)CATH (3hua)Enterobacteria phage T4
3huk, downloadSCOP (3huk)CATH (3huk)Enterobacteria phage T4
3huq, downloadSCOP (3huq)CATH (3huq)Enterobacteria phage T4
3hwl, downloadSCOP (3hwl)CATH (3hwl)Enterobacteria phage T4
3jr6, downloadSCOP (3jr6)CATH (3jr6)Enterobacteria phage T4
3k2r, downloadSCOP (3k2r)CATH (3k2r)Enterobacteria phage T4
3l2x, downloadSCOP (3l2x)CATH (3l2x)Enterobacteria phage T4
3l64, downloadSCOP (3l64)CATH (3l64)Enterobacteria phage T4
3lzm, downloadSCOP (3lzm)CATH (3lzm)Enterobacteria phage T4
3odu, downloadSCOP (3odu)CATH (3odu)Enterobacteria phage T4
3oe0, downloadSCOP (3oe0)CATH (3oe0)Enterobacteria phage T4
3oe6, downloadSCOP (3oe6)CATH (3oe6)Enterobacteria phage T4
3oe8, downloadSCOP (3oe8)CATH (3oe8)Enterobacteria phage T4
3oe9, downloadSCOP (3oe9)CATH (3oe9)Enterobacteria phage T4
3p0g, downloadSCOP (3p0g)CATH (3p0g)Enterobacteria phage T4
3pbl, downloadSCOP (3pbl)CATH (3pbl)Enterobacteria phage T4
3pds, downloadSCOP (3pds)CATH (3pds)Enterobacteria phage T4
3qak, downloadSCOP (3qak)CATH (3qak)Enterobacteria phage T4
3run, downloadSCOP (3run)CATH (3run)Enterobacteria phage T4
3rze, downloadSCOP (3rze)CATH (3rze)Enterobacteria phage T4
3sb5, downloadSCOP (3sb5)CATH (3sb5)Enterobacteria phage T4
3sb6, downloadSCOP (3sb6)CATH (3sb6)Enterobacteria phage T4
3sb7, downloadSCOP (3sb7)CATH (3sb7)Enterobacteria phage T4
3sb8, downloadSCOP (3sb8)CATH (3sb8)Enterobacteria phage T4
3sb9, downloadSCOP (3sb9)CATH (3sb9)Enterobacteria phage T4
3sba, downloadSCOP (3sba)CATH (3sba)Enterobacteria phage T4
3sbb, downloadSCOP (3sbb)CATH (3sbb)Enterobacteria phage T4
3uon, downloadSCOP (3uon)CATH (3uon)Enterobacteria phage T4
3v2w, downloadSCOP (3v2w)CATH (3v2w)Enterobacteria phage T4
3v2y, downloadSCOP (3v2y)CATH (3v2y)Enterobacteria phage T4
3vw7, downloadSCOP (3vw7)CATH (3vw7)Enterobacteria phage T4
4daj, downloadSCOP (4daj)CATH (4daj)Enterobacteria phage T4
4dkl, downloadSCOP (4dkl)CATH (4dkl)Enterobacteria phage T4
4e97, downloadSCOP (4e97)CATH (4e97)Enterobacteria phage T4
4ej4, downloadSCOP (4ej4)CATH (4ej4)Enterobacteria phage T4
4ekp, downloadSCOP (4ekp)CATH (4ekp)Enterobacteria phage T4
4ekq, downloadSCOP (4ekq)CATH (4ekq)Enterobacteria phage T4
4ekr, downloadSCOP (4ekr)CATH (4ekr)Enterobacteria phage T4
4eks, downloadSCOP (4eks)CATH (4eks)Enterobacteria phage T4
4gbr, downloadSCOP (4gbr)CATH (4gbr)Enterobacteria phage T4
4lzm, downloadSCOP (4lzm)CATH (4lzm)Enterobacteria phage T4
5lzm, downloadSCOP (5lzm)CATH (5lzm)Enterobacteria phage T4
6lzm, downloadSCOP (6lzm)CATH (6lzm)Enterobacteria phage T4
7lzm, downloadSCOP (7lzm)CATH (7lzm)Enterobacteria phage T4
3gxk, downloadSCOP (3gxk)CATH (3gxk)Gadus morhua
3gxr, downloadSCOP (3gxr)CATH (3gxr)Gadus morhua
132l, downloadSCOP (132l)CATH (132l)Gallus gallus
1a2y, downloadSCOP (1a2y)CATH (1a2y)Gallus gallus
1aki, downloadSCOP (1aki)CATH (1aki)Gallus gallus
1at5, downloadSCOP (1at5)CATH (1at5)Gallus gallus
1at6, downloadSCOP (1at6)CATH (1at6)Gallus gallus
1azf, downloadSCOP (1azf)CATH (1azf)Gallus gallus
1b0d, downloadSCOP (1b0d)CATH (1b0d)Gallus gallus
1b2k, downloadSCOP (1b2k)CATH (1b2k)Gallus gallus
1bgi, downloadSCOP (1bgi)CATH (1bgi)Gallus gallus
1bhz, downloadSCOP (1bhz)CATH (1bhz)Gallus gallus
1bvk, downloadSCOP (1bvk)CATH (1bvk)Gallus gallus
1bvx, downloadSCOP (1bvx)CATH (1bvx)Gallus gallus
1bwh, downloadSCOP (1bwh)CATH (1bwh)Gallus gallus
1bwi, downloadSCOP (1bwi)CATH (1bwi)Gallus gallus
1bwj, downloadSCOP (1bwj)CATH (1bwj)Gallus gallus
1c10, downloadSCOP (1c10)CATH (1c10)Gallus gallus
1dpw, downloadSCOP (1dpw)CATH (1dpw)Gallus gallus
1dpx, downloadSCOP (1dpx)CATH (1dpx)Gallus gallus
1dqj, downloadSCOP (1dqj)CATH (1dqj)Gallus gallus
1e8l, downloadSCOP (1e8l)CATH (1e8l)Gallus gallus
1f0w, downloadSCOP (1f0w)CATH (1f0w)Gallus gallus
1f10, downloadSCOP (1f10)CATH (1f10)Gallus gallus
1fdl, downloadSCOP (1fdl)CATH (1fdl)Gallus gallus
1flq, downloadSCOP (1flq)CATH (1flq)Gallus gallus
1flu, downloadSCOP (1flu)CATH (1flu)Gallus gallus
1flw, downloadSCOP (1flw)CATH (1flw)Gallus gallus
1fly, downloadSCOP (1fly)CATH (1fly)Gallus gallus
1fn5, downloadSCOP (1fn5)CATH (1fn5)Gallus gallus
1g7h, downloadSCOP (1g7h)CATH (1g7h)Gallus gallus
1g7i, downloadSCOP (1g7i)CATH (1g7i)Gallus gallus
1g7j, downloadSCOP (1g7j)CATH (1g7j)Gallus gallus
1g7l, downloadSCOP (1g7l)CATH (1g7l)Gallus gallus
1g7m, downloadSCOP (1g7m)CATH (1g7m)Gallus gallus
1gpq, downloadSCOP (1gpq)CATH (1gpq)Gallus gallus
1gwd, downloadSCOP (1gwd)CATH (1gwd)Gallus gallus
1gxv, downloadSCOP (1gxv)CATH (1gxv)Gallus gallus
1gxx, downloadSCOP (1gxx)CATH (1gxx)Gallus gallus
1h6m, downloadSCOP (1h6m)CATH (1h6m)Gallus gallus
1h87, downloadSCOP (1h87)CATH (1h87)Gallus gallus
1hc0, downloadSCOP (1hc0)CATH (1hc0)Gallus gallus
1hel, downloadSCOP (1hel)CATH (1hel)Gallus gallus
1hem, downloadSCOP (1hem)CATH (1hem)Gallus gallus
1hen, downloadSCOP (1hen)CATH (1hen)Gallus gallus
1heo, downloadSCOP (1heo)CATH (1heo)Gallus gallus
1hep, downloadSCOP (1hep)CATH (1hep)Gallus gallus
1heq, downloadSCOP (1heq)CATH (1heq)Gallus gallus
1her, downloadSCOP (1her)CATH (1her)Gallus gallus
1hew, downloadSCOP (1hew)CATH (1hew)Gallus gallus
1hf4, downloadSCOP (1hf4)CATH (1hf4)Gallus gallus
1hsw, downloadSCOP (1hsw)CATH (1hsw)Gallus gallus
1hsx, downloadSCOP (1hsx)CATH (1hsx)Gallus gallus
1ic4, downloadSCOP (1ic4)CATH (1ic4)Gallus gallus
1ic5, downloadSCOP (1ic5)CATH (1ic5)Gallus gallus
1ic7, downloadSCOP (1ic7)CATH (1ic7)Gallus gallus
1iee, downloadSCOP (1iee)CATH (1iee)Gallus gallus
1io5, downloadSCOP (1io5)CATH (1io5)Gallus gallus
1ioq, downloadSCOP (1ioq)CATH (1ioq)Gallus gallus
1ior, downloadSCOP (1ior)CATH (1ior)Gallus gallus
1ios, downloadSCOP (1ios)CATH (1ios)Gallus gallus
1ir7, downloadSCOP (1ir7)CATH (1ir7)Gallus gallus
1ir8, downloadSCOP (1ir8)CATH (1ir8)Gallus gallus
1ir9, downloadSCOP (1ir9)CATH (1ir9)Gallus gallus
1j1o, downloadSCOP (1j1o)CATH (1j1o)Gallus gallus
1j1p, downloadSCOP (1j1p)CATH (1j1p)Gallus gallus
1j1x, downloadSCOP (1j1x)CATH (1j1x)Gallus gallus
1ja2, downloadSCOP (1ja2)CATH (1ja2)Gallus gallus
1ja4, downloadSCOP (1ja4)CATH (1ja4)Gallus gallus
1ja6, downloadSCOP (1ja6)CATH (1ja6)Gallus gallus
1ja7, downloadSCOP (1ja7)CATH (1ja7)Gallus gallus
1jis, downloadSCOP (1jis)CATH (1jis)Gallus gallus
1jit, downloadSCOP (1jit)CATH (1jit)Gallus gallus
1jiy, downloadSCOP (1jiy)CATH (1jiy)Gallus gallus
1jj0, downloadSCOP (1jj0)CATH (1jj0)Gallus gallus
1jj1, downloadSCOP (1jj1)CATH (1jj1)Gallus gallus
1jj3, downloadSCOP (1jj3)CATH (1jj3)Gallus gallus
1jpo, downloadSCOP (1jpo)CATH (1jpo)Gallus gallus
1jto, downloadSCOP (1jto)CATH (1jto)Gallus gallus
1jtt, downloadSCOP (1jtt)CATH (1jtt)Gallus gallus
1kip, downloadSCOP (1kip)CATH (1kip)Gallus gallus
1kiq, downloadSCOP (1kiq)CATH (1kiq)Gallus gallus
1kir, downloadSCOP (1kir)CATH (1kir)Gallus gallus
1kxw, downloadSCOP (1kxw)CATH (1kxw)Gallus gallus
1kxx, downloadSCOP (1kxx)CATH (1kxx)Gallus gallus
1kxy, downloadSCOP (1kxy)CATH (1kxy)Gallus gallus
1lcn, downloadSCOP (1lcn)CATH (1lcn)Gallus gallus
1lj3, downloadSCOP (1lj3)CATH (1lj3)Gallus gallus
1lj4, downloadSCOP (1lj4)CATH (1lj4)Gallus gallus
1lje, downloadSCOP (1lje)CATH (1lje)Gallus gallus
1ljf, downloadSCOP (1ljf)CATH (1ljf)Gallus gallus
1ljg, downloadSCOP (1ljg)CATH (1ljg)Gallus gallus
1ljh, downloadSCOP (1ljh)CATH (1ljh)Gallus gallus
1lji, downloadSCOP (1lji)CATH (1lji)Gallus gallus
1ljj, downloadSCOP (1ljj)CATH (1ljj)Gallus gallus
1ljk, downloadSCOP (1ljk)CATH (1ljk)Gallus gallus
1lkr, downloadSCOP (1lkr)CATH (1lkr)Gallus gallus
1lks, downloadSCOP (1lks)CATH (1lks)Gallus gallus
1lma, downloadSCOP (1lma)CATH (1lma)Gallus gallus
1lpi, downloadSCOP (1lpi)CATH (1lpi)Gallus gallus
1lsa, downloadSCOP (1lsa)CATH (1lsa)Gallus gallus
1lsb, downloadSCOP (1lsb)CATH (1lsb)Gallus gallus
1lsc, downloadSCOP (1lsc)CATH (1lsc)Gallus gallus
1lsd, downloadSCOP (1lsd)CATH (1lsd)Gallus gallus
1lse, downloadSCOP (1lse)CATH (1lse)Gallus gallus
1lsf, downloadSCOP (1lsf)CATH (1lsf)Gallus gallus
1lsm, downloadSCOP (1lsm)CATH (1lsm)Gallus gallus
1lsn, downloadSCOP (1lsn)CATH (1lsn)Gallus gallus
1lsy, downloadSCOP (1lsy)CATH (1lsy)Gallus gallus
1lsz, downloadSCOP (1lsz)CATH (1lsz)Gallus gallus
1lyo, downloadSCOP (1lyo)CATH (1lyo)Gallus gallus
1lys, downloadSCOP (1lys)CATH (1lys)Gallus gallus
1lyz, downloadSCOP (1lyz)CATH (1lyz)Gallus gallus
1lz8, downloadSCOP (1lz8)CATH (1lz8)Gallus gallus
1lz9, downloadSCOP (1lz9)CATH (1lz9)Gallus gallus
1lza, downloadSCOP (1lza)CATH (1lza)Gallus gallus
1lzb, downloadSCOP (1lzb)CATH (1lzb)Gallus gallus
1lzc, downloadSCOP (1lzc)CATH (1lzc)Gallus gallus
1lzd, downloadSCOP (1lzd)CATH (1lzd)Gallus gallus
1lze, downloadSCOP (1lze)CATH (1lze)Gallus gallus
1lzg, downloadSCOP (1lzg)CATH (1lzg)Gallus gallus
1lzh, downloadSCOP (1lzh)CATH (1lzh)Gallus gallus
1lzn, downloadSCOP (1lzn)CATH (1lzn)Gallus gallus
1lzt, downloadSCOP (1lzt)CATH (1lzt)Gallus gallus
1mel, downloadSCOP (1mel)CATH (1mel)Gallus gallus
1n4f, downloadSCOP (1n4f)CATH (1n4f)Gallus gallus
1nby, downloadSCOP (1nby)CATH (1nby)Gallus gallus
1nbz, downloadSCOP (1nbz)CATH (1nbz)Gallus gallus
1ndg, downloadSCOP (1ndg)CATH (1ndg)Gallus gallus
1ndm, downloadSCOP (1ndm)CATH (1ndm)Gallus gallus
1p2c, downloadSCOP (1p2c)CATH (1p2c)Gallus gallus
1ps5, downloadSCOP (1ps5)CATH (1ps5)Gallus gallus
1qio, downloadSCOP (1qio)CATH (1qio)Gallus gallus
1qtk, downloadSCOP (1qtk)CATH (1qtk)Gallus gallus
1rcm, downloadSCOP (1rcm)CATH (1rcm)Gallus gallus
1rfp, downloadSCOP (1rfp)CATH (1rfp)Gallus gallus
1ri8, downloadSCOP (1ri8)CATH (1ri8)Gallus gallus
1rjc, downloadSCOP (1rjc)CATH (1rjc)Gallus gallus
1sf4, downloadSCOP (1sf4)CATH (1sf4)Gallus gallus
1sf6, downloadSCOP (1sf6)CATH (1sf6)Gallus gallus
1sf7, downloadSCOP (1sf7)CATH (1sf7)Gallus gallus
1sfb, downloadSCOP (1sfb)CATH (1sfb)Gallus gallus
1sfg, downloadSCOP (1sfg)CATH (1sfg)Gallus gallus
1sq2, downloadSCOP (1sq2)CATH (1sq2)Gallus gallus
1t3p, downloadSCOP (1t3p)CATH (1t3p)Gallus gallus
1t6v, downloadSCOP (1t6v)CATH (1t6v)Gallus gallus
1ua6, downloadSCOP (1ua6)CATH (1ua6)Gallus gallus
1uc0, downloadSCOP (1uc0)CATH (1uc0)Gallus gallus
1uco, downloadSCOP (1uco)CATH (1uco)Gallus gallus
1uia, downloadSCOP (1uia)CATH (1uia)Gallus gallus
1uib, downloadSCOP (1uib)CATH (1uib)Gallus gallus
1uic, downloadSCOP (1uic)CATH (1uic)Gallus gallus
1uid, downloadSCOP (1uid)CATH (1uid)Gallus gallus
1uie, downloadSCOP (1uie)CATH (1uie)Gallus gallus
1uif, downloadSCOP (1uif)CATH (1uif)Gallus gallus
1uig, downloadSCOP (1uig)CATH (1uig)Gallus gallus
1uih, downloadSCOP (1uih)CATH (1uih)Gallus gallus
1uuz, downloadSCOP (1uuz)CATH (1uuz)Gallus gallus
1v7s, downloadSCOP (1v7s)CATH (1v7s)Gallus gallus
1v7t, downloadSCOP (1v7t)CATH (1v7t)Gallus gallus
1vat, downloadSCOP (1vat)CATH (1vat)Gallus gallus
1vau, downloadSCOP (1vau)CATH (1vau)Gallus gallus
1vdp, downloadSCOP (1vdp)CATH (1vdp)Gallus gallus
1vdq, downloadSCOP (1vdq)CATH (1vdq)Gallus gallus
1vds, downloadSCOP (1vds)CATH (1vds)Gallus gallus
1vdt, downloadSCOP (1vdt)CATH (1vdt)Gallus gallus
1ved, downloadSCOP (1ved)CATH (1ved)Gallus gallus
1w6z, downloadSCOP (1w6z)CATH (1w6z)Gallus gallus
1wtm, downloadSCOP (1wtm)CATH (1wtm)Gallus gallus
1wtn, downloadSCOP (1wtn)CATH (1wtn)Gallus gallus
1xei, downloadSCOP (1xei)CATH (1xei)Gallus gallus
1xej, downloadSCOP (1xej)CATH (1xej)Gallus gallus
1xek, downloadSCOP (1xek)CATH (1xek)Gallus gallus
1xfp, downloadSCOP (1xfp)CATH (1xfp)Gallus gallus
1xgp, downloadSCOP (1xgp)CATH (1xgp)Gallus gallus
1xgq, downloadSCOP (1xgq)CATH (1xgq)Gallus gallus
1yik, downloadSCOP (1yik)CATH (1yik)Gallus gallus
1yil, downloadSCOP (1yil)CATH (1yil)Gallus gallus
1ykx, downloadSCOP (1ykx)CATH (1ykx)Gallus gallus
1yky, downloadSCOP (1yky)CATH (1yky)Gallus gallus
1ykz, downloadSCOP (1ykz)CATH (1ykz)Gallus gallus
1yl0, downloadSCOP (1yl0)CATH (1yl0)Gallus gallus
1yl1, downloadSCOP (1yl1)CATH (1yl1)Gallus gallus
1yqv, downloadSCOP (1yqv)CATH (1yqv)Gallus gallus
1z55, downloadSCOP (1z55)CATH (1z55)Gallus gallus
1zmy, downloadSCOP (1zmy)CATH (1zmy)Gallus gallus
1zv5, downloadSCOP (1zv5)CATH (1zv5)Gallus gallus
1zvh, downloadSCOP (1zvh)CATH (1zvh)Gallus gallus
1zvy, downloadSCOP (1zvy)CATH (1zvy)Gallus gallus
2a6u, downloadSCOP (2a6u)CATH (2a6u)Gallus gallus
2a7d, downloadSCOP (2a7d)CATH (2a7d)Gallus gallus
2a7f, downloadSCOP (2a7f)CATH (2a7f)Gallus gallus
2aub, downloadSCOP (2aub)CATH (2aub)Gallus gallus
2b5z, downloadSCOP (2b5z)CATH (2b5z)Gallus gallus
2blx, downloadSCOP (2blx)CATH (2blx)Gallus gallus
2bly, downloadSCOP (2bly)CATH (2bly)Gallus gallus
2bpu, downloadSCOP (2bpu)CATH (2bpu)Gallus gallus
2c8o, downloadSCOP (2c8o)CATH (2c8o)Gallus gallus
2c8p, downloadSCOP (2c8p)CATH (2c8p)Gallus gallus
2cds, downloadSCOP (2cds)CATH (2cds)Gallus gallus
2cgi, downloadSCOP (2cgi)CATH (2cgi)Gallus gallus
2d4i, downloadSCOP (2d4i)CATH (2d4i)Gallus gallus
2d4j, downloadSCOP (2d4j)CATH (2d4j)Gallus gallus
2d4k, downloadSCOP (2d4k)CATH (2d4k)Gallus gallus
2d6b, downloadSCOP (2d6b)CATH (2d6b)Gallus gallus
2d91, downloadSCOP (2d91)CATH (2d91)Gallus gallus
2dqc, downloadSCOP (2dqc)CATH (2dqc)Gallus gallus
2dqd, downloadSCOP (2dqd)CATH (2dqd)Gallus gallus
2dqe, downloadSCOP (2dqe)CATH (2dqe)Gallus gallus
2dqf, downloadSCOP (2dqf)CATH (2dqf)Gallus gallus
2dqg, downloadSCOP (2dqg)CATH (2dqg)Gallus gallus
2dqh, downloadSCOP (2dqh)CATH (2dqh)Gallus gallus
2dqi, downloadSCOP (2dqi)CATH (2dqi)Gallus gallus
2dqj, downloadSCOP (2dqj)CATH (2dqj)Gallus gallus
2eiz, downloadSCOP (2eiz)CATH (2eiz)Gallus gallus
2eks, downloadSCOP (2eks)CATH (2eks)Gallus gallus
2epe, downloadSCOP (2epe)CATH (2epe)Gallus gallus
2f2n, downloadSCOP (2f2n)CATH (2f2n)Gallus gallus
2f30, downloadSCOP (2f30)CATH (2f30)Gallus gallus
2f4a, downloadSCOP (2f4a)CATH (2f4a)Gallus gallus
2f4g, downloadSCOP (2f4g)CATH (2f4g)Gallus gallus
2fbb, downloadSCOP (2fbb)CATH (2fbb)Gallus gallus
2g4p, downloadSCOP (2g4p)CATH (2g4p)Gallus gallus
2g4q, downloadSCOP (2g4q)CATH (2g4q)Gallus gallus
2h9j, downloadSCOP (2h9j)CATH (2h9j)Gallus gallus
2h9k, downloadSCOP (2h9k)CATH (2h9k)Gallus gallus
2hfm, downloadSCOP (2hfm)CATH (2hfm)Gallus gallus
2hs7, downloadSCOP (2hs7)CATH (2hs7)Gallus gallus
2hs9, downloadSCOP (2hs9)CATH (2hs9)Gallus gallus
2hso, downloadSCOP (2hso)CATH (2hso)Gallus gallus
2htx, downloadSCOP (2htx)CATH (2htx)Gallus gallus
2hu1, downloadSCOP (2hu1)CATH (2hu1)Gallus gallus
2hu3, downloadSCOP (2hu3)CATH (2hu3)Gallus gallus
2hub, downloadSCOP (2hub)CATH (2hub)Gallus gallus
2i25, downloadSCOP (2i25)CATH (2i25)Gallus gallus
2i26, downloadSCOP (2i26)CATH (2i26)Gallus gallus
2i6z, downloadSCOP (2i6z)CATH (2i6z)Gallus gallus
2lym, downloadSCOP (2lym)CATH (2lym)Gallus gallus
2lyo, downloadSCOP (2lyo)CATH (2lyo)Gallus gallus
2lyz, downloadSCOP (2lyz)CATH (2lyz)Gallus gallus
2lzh, downloadSCOP (2lzh)CATH (2lzh)Gallus gallus
2lzt, downloadSCOP (2lzt)CATH (2lzt)Gallus gallus
2pc2, downloadSCOP (2pc2)CATH (2pc2)Gallus gallus
2q0m, downloadSCOP (2q0m)CATH (2q0m)Gallus gallus
2vb1, downloadSCOP (2vb1)CATH (2vb1)Gallus gallus
2w1l, downloadSCOP (2w1l)CATH (2w1l)Gallus gallus
2w1m, downloadSCOP (2w1m)CATH (2w1m)Gallus gallus
2w1x, downloadSCOP (2w1x)CATH (2w1x)Gallus gallus
2w1y, downloadSCOP (2w1y)CATH (2w1y)Gallus gallus
2war, downloadSCOP (2war)CATH (2war)Gallus gallus
2x0a, downloadSCOP (2x0a)CATH (2x0a)Gallus gallus
2xbr, downloadSCOP (2xbr)CATH (2xbr)Gallus gallus
2xbs, downloadSCOP (2xbs)CATH (2xbs)Gallus gallus
2xjw, downloadSCOP (2xjw)CATH (2xjw)Gallus gallus
2xth, downloadSCOP (2xth)CATH (2xth)Gallus gallus
2ybh, downloadSCOP (2ybh)CATH (2ybh)Gallus gallus
2ybi, downloadSCOP (2ybi)CATH (2ybi)Gallus gallus
2ybj, downloadSCOP (2ybj)CATH (2ybj)Gallus gallus
2ybl, downloadSCOP (2ybl)CATH (2ybl)Gallus gallus
2ybm, downloadSCOP (2ybm)CATH (2ybm)Gallus gallus
2ybn, downloadSCOP (2ybn)CATH (2ybn)Gallus gallus
2ydg, downloadSCOP (2ydg)CATH (2ydg)Gallus gallus
2yss, downloadSCOP (2yss)CATH (2yss)Gallus gallus
2yvb, downloadSCOP (2yvb)CATH (2yvb)Gallus gallus
2z12, downloadSCOP (2z12)CATH (2z12)Gallus gallus
2z18, downloadSCOP (2z18)CATH (2z18)Gallus gallus
2z19, downloadSCOP (2z19)CATH (2z19)Gallus gallus
2znw, downloadSCOP (2znw)CATH (2znw)Gallus gallus
2znx, downloadSCOP (2znx)CATH (2znx)Gallus gallus
2zq3, downloadSCOP (2zq3)CATH (2zq3)Gallus gallus
2zq4, downloadSCOP (2zq4)CATH (2zq4)Gallus gallus
2zyp, downloadSCOP (2zyp)CATH (2zyp)Gallus gallus
3a34, downloadSCOP (3a34)CATH (3a34)Gallus gallus
3a3q, downloadSCOP (3a3q)CATH (3a3q)Gallus gallus
3a3r, downloadSCOP (3a3r)CATH (3a3r)Gallus gallus
3a67, downloadSCOP (3a67)CATH (3a67)Gallus gallus
3a6b, downloadSCOP (3a6b)CATH (3a6b)Gallus gallus
3a6c, downloadSCOP (3a6c)CATH (3a6c)Gallus gallus
3a8z, downloadSCOP (3a8z)CATH (3a8z)Gallus gallus
3a90, downloadSCOP (3a90)CATH (3a90)Gallus gallus
3a91, downloadSCOP (3a91)CATH (3a91)Gallus gallus
3a92, downloadSCOP (3a92)CATH (3a92)Gallus gallus
3a93, downloadSCOP (3a93)CATH (3a93)Gallus gallus
3a94, downloadSCOP (3a94)CATH (3a94)Gallus gallus
3a95, downloadSCOP (3a95)CATH (3a95)Gallus gallus
3a96, downloadSCOP (3a96)CATH (3a96)Gallus gallus
3agg, downloadSCOP (3agg)CATH (3agg)Gallus gallus
3agh, downloadSCOP (3agh)CATH (3agh)Gallus gallus
3agi, downloadSCOP (3agi)CATH (3agi)Gallus gallus
3ajn, downloadSCOP (3ajn)CATH (3ajn)Gallus gallus
3atn, downloadSCOP (3atn)CATH (3atn)Gallus gallus
3ato, downloadSCOP (3ato)CATH (3ato)Gallus gallus
3aw6, downloadSCOP (3aw6)CATH (3aw6)Gallus gallus
3aw7, downloadSCOP (3aw7)CATH (3aw7)Gallus gallus
3az4, downloadSCOP (3az4)CATH (3az4)Gallus gallus
3az5, downloadSCOP (3az5)CATH (3az5)Gallus gallus
3az6, downloadSCOP (3az6)CATH (3az6)Gallus gallus
3az7, downloadSCOP (3az7)CATH (3az7)Gallus gallus
3b6l, downloadSCOP (3b6l)CATH (3b6l)Gallus gallus
3b72, downloadSCOP (3b72)CATH (3b72)Gallus gallus
3d9a, downloadSCOP (3d9a)CATH (3d9a)Gallus gallus
3e3d, downloadSCOP (3e3d)CATH (3e3d)Gallus gallus
3ems, downloadSCOP (3ems)CATH (3ems)Gallus gallus
3exd, downloadSCOP (3exd)CATH (3exd)Gallus gallus
3f6z, downloadSCOP (3f6z)CATH (3f6z)Gallus gallus
3g3a, downloadSCOP (3g3a)CATH (3g3a)Gallus gallus
3g3b, downloadSCOP (3g3b)CATH (3g3b)Gallus gallus
3hfm, downloadSCOP (3hfm)CATH (3hfm)Gallus gallus
3iju, downloadSCOP (3iju)CATH (3iju)Gallus gallus
3ijv, downloadSCOP (3ijv)CATH (3ijv)Gallus gallus
3kam, downloadSCOP (3kam)CATH (3kam)Gallus gallus
3lym, downloadSCOP (3lym)CATH (3lym)Gallus gallus
3lyo, downloadSCOP (3lyo)CATH (3lyo)Gallus gallus
3lyt, downloadSCOP (3lyt)CATH (3lyt)Gallus gallus
3lyz, downloadSCOP (3lyz)CATH (3lyz)Gallus gallus
3lzt, downloadSCOP (3lzt)CATH (3lzt)Gallus gallus
3m18, downloadSCOP (3m18)CATH (3m18)Gallus gallus
3m3u, downloadSCOP (3m3u)CATH (3m3u)Gallus gallus
3n9a, downloadSCOP (3n9a)CATH (3n9a)Gallus gallus
3n9c, downloadSCOP (3n9c)CATH (3n9c)Gallus gallus
3n9e, downloadSCOP (3n9e)CATH (3n9e)Gallus gallus
3ojp, downloadSCOP (3ojp)CATH (3ojp)Gallus gallus
3ok0, downloadSCOP (3ok0)CATH (3ok0)Gallus gallus
3otp, downloadSCOP (3otp)CATH (3otp)Gallus gallus
3p4z, downloadSCOP (3p4z)CATH (3p4z)Gallus gallus
3p64, downloadSCOP (3p64)CATH (3p64)Gallus gallus
3p65, downloadSCOP (3p65)CATH (3p65)Gallus gallus
3p66, downloadSCOP (3p66)CATH (3p66)Gallus gallus
3p68, downloadSCOP (3p68)CATH (3p68)Gallus gallus
3qe8, downloadSCOP (3qe8)CATH (3qe8)Gallus gallus
3qng, downloadSCOP (3qng)CATH (3qng)Gallus gallus
3qy4, downloadSCOP (3qy4)CATH (3qy4)Gallus gallus
3rnx, downloadSCOP (3rnx)CATH (3rnx)Gallus gallus
3rt5, downloadSCOP (3rt5)CATH (3rt5)Gallus gallus
3ru5, downloadSCOP (3ru5)CATH (3ru5)Gallus gallus
3rw8, downloadSCOP (3rw8)CATH (3rw8)Gallus gallus
3rz4, downloadSCOP (3rz4)CATH (3rz4)Gallus gallus
3sp3, downloadSCOP (3sp3)CATH (3sp3)Gallus gallus
3t6u, downloadSCOP (3t6u)CATH (3t6u)Gallus gallus
3tmu, downloadSCOP (3tmu)CATH (3tmu)Gallus gallus
3tmv, downloadSCOP (3tmv)CATH (3tmv)Gallus gallus
3tmw, downloadSCOP (3tmw)CATH (3tmw)Gallus gallus
3tmx, downloadSCOP (3tmx)CATH (3tmx)Gallus gallus
3ulr, downloadSCOP (3ulr)CATH (3ulr)Gallus gallus
3zvq, downloadSCOP (3zvq)CATH (3zvq)Gallus gallus
4a7d, downloadSCOP (4a7d)CATH (4a7d)Gallus gallus
4a8a, downloadSCOP (4a8a)CATH (4a8a)Gallus gallus
4a8b, downloadSCOP (4a8b)CATH (4a8b)Gallus gallus
4aga, downloadSCOP (4aga)CATH (4aga)Gallus gallus
4axt, downloadSCOP (4axt)CATH (4axt)Gallus gallus
4b0d, downloadSCOP (4b0d)CATH (4b0d)Gallus gallus
4b49, downloadSCOP (4b49)CATH (4b49)Gallus gallus
4b4e, downloadSCOP (4b4e)CATH (4b4e)Gallus gallus
4b4i, downloadSCOP (4b4i)CATH (4b4i)Gallus gallus
4b4j, downloadSCOP (4b4j)CATH (4b4j)Gallus gallus
4bad, downloadSCOP (4bad)CATH (4bad)Gallus gallus
4baf, downloadSCOP (4baf)CATH (4baf)Gallus gallus
4bap, downloadSCOP (4bap)CATH (4bap)Gallus gallus
4dd0, downloadSCOP (4dd0)CATH (4dd0)Gallus gallus
4dd1, downloadSCOP (4dd1)CATH (4dd1)Gallus gallus
4dd2, downloadSCOP (4dd2)CATH (4dd2)Gallus gallus
4dd3, downloadSCOP (4dd3)CATH (4dd3)Gallus gallus
4dd4, downloadSCOP (4dd4)CATH (4dd4)Gallus gallus
4dd6, downloadSCOP (4dd6)CATH (4dd6)Gallus gallus
4dd7, downloadSCOP (4dd7)CATH (4dd7)Gallus gallus
4dd9, downloadSCOP (4dd9)CATH (4dd9)Gallus gallus
4dda, downloadSCOP (4dda)CATH (4dda)Gallus gallus
4ddb, downloadSCOP (4ddb)CATH (4ddb)Gallus gallus
4ddc, downloadSCOP (4ddc)CATH (4ddc)Gallus gallus
4dt3, downloadSCOP (4dt3)CATH (4dt3)Gallus gallus
4e3u, downloadSCOP (4e3u)CATH (4e3u)Gallus gallus
4et8, downloadSCOP (4et8)CATH (4et8)Gallus gallus
4et9, downloadSCOP (4et9)CATH (4et9)Gallus gallus
4eta, downloadSCOP (4eta)CATH (4eta)Gallus gallus
4etb, downloadSCOP (4etb)CATH (4etb)Gallus gallus
4etc, downloadSCOP (4etc)CATH (4etc)Gallus gallus
4etd, downloadSCOP (4etd)CATH (4etd)Gallus gallus
4ete, downloadSCOP (4ete)CATH (4ete)Gallus gallus
4g49, downloadSCOP (4g49)CATH (4g49)Gallus gallus
4g4a, downloadSCOP (4g4a)CATH (4g4a)Gallus gallus
4g4b, downloadSCOP (4g4b)CATH (4g4b)Gallus gallus
4g4c, downloadSCOP (4g4c)CATH (4g4c)Gallus gallus
4g4h, downloadSCOP (4g4h)CATH (4g4h)Gallus gallus
4h1p, downloadSCOP (4h1p)CATH (4h1p)Gallus gallus
4lym, downloadSCOP (4lym)CATH (4lym)Gallus gallus
4lyo, downloadSCOP (4lyo)CATH (4lyo)Gallus gallus
4lyt, downloadSCOP (4lyt)CATH (4lyt)Gallus gallus
4lyz, downloadSCOP (4lyz)CATH (4lyz)Gallus gallus
4lzt, downloadSCOP (4lzt)CATH (4lzt)Gallus gallus
5lym, downloadSCOP (5lym)CATH (5lym)Gallus gallus
5lyt, downloadSCOP (5lyt)CATH (5lyt)Gallus gallus
5lyz, downloadSCOP (5lyz)CATH (5lyz)Gallus gallus
6lyt, downloadSCOP (6lyt)CATH (6lyt)Gallus gallus
6lyz, downloadSCOP (6lyz)CATH (6lyz)Gallus gallus
7lyz, downloadSCOP (7lyz)CATH (7lyz)Gallus gallus
8lyz, downloadSCOP (8lyz)CATH (8lyz)Gallus gallus
9lyz, downloadSCOP (9lyz)CATH (9lyz)Gallus gallus
1hvq, downloadSCOP (1hvq)CATH (1hvq)Hevea brasiliensis
1kqy, downloadSCOP (1kqy)CATH (1kqy)Hevea brasiliensis
1kqz, downloadSCOP (1kqz)CATH (1kqz)Hevea brasiliensis
1kr0, downloadSCOP (1kr0)CATH (1kr0)Hevea brasiliensis
1kr1, downloadSCOP (1kr1)CATH (1kr1)Hevea brasiliensis
1llo, downloadSCOP (1llo)CATH (1llo)Hevea brasiliensis
2hvm, downloadSCOP (2hvm)CATH (2hvm)Hevea brasiliensis
133l, downloadSCOP (133l)CATH (133l)Homo sapiens
134l, downloadSCOP (134l)CATH (134l)Homo sapiens
1b5u, downloadSCOP (1b5u)CATH (1b5u)Homo sapiens
1b5v, downloadSCOP (1b5v)CATH (1b5v)Homo sapiens
1b5w, downloadSCOP (1b5w)CATH (1b5w)Homo sapiens
1b5x, downloadSCOP (1b5x)CATH (1b5x)Homo sapiens
1b5y, downloadSCOP (1b5y)CATH (1b5y)Homo sapiens
1b5z, downloadSCOP (1b5z)CATH (1b5z)Homo sapiens
1b7l, downloadSCOP (1b7l)CATH (1b7l)Homo sapiens
1b7m, downloadSCOP (1b7m)CATH (1b7m)Homo sapiens
1b7n, downloadSCOP (1b7n)CATH (1b7n)Homo sapiens
1b7o, downloadSCOP (1b7o)CATH (1b7o)Homo sapiens
1b7p, downloadSCOP (1b7p)CATH (1b7p)Homo sapiens
1b7q, downloadSCOP (1b7q)CATH (1b7q)Homo sapiens
1b7r, downloadSCOP (1b7r)CATH (1b7r)Homo sapiens
1bb3, downloadSCOP (1bb3)CATH (1bb3)Homo sapiens
1bb4, downloadSCOP (1bb4)CATH (1bb4)Homo sapiens
1bb5, downloadSCOP (1bb5)CATH (1bb5)Homo sapiens
1c43, downloadSCOP (1c43)CATH (1c43)Homo sapiens
1c45, downloadSCOP (1c45)CATH (1c45)Homo sapiens
1c46, downloadSCOP (1c46)CATH (1c46)Homo sapiens
1c7p, downloadSCOP (1c7p)CATH (1c7p)Homo sapiens
1cj6, downloadSCOP (1cj6)CATH (1cj6)Homo sapiens
1cj7, downloadSCOP (1cj7)CATH (1cj7)Homo sapiens
1cj8, downloadSCOP (1cj8)CATH (1cj8)Homo sapiens
1cj9, downloadSCOP (1cj9)CATH (1cj9)Homo sapiens
1ckc, downloadSCOP (1ckc)CATH (1ckc)Homo sapiens
1ckd, downloadSCOP (1ckd)CATH (1ckd)Homo sapiens
1ckf, downloadSCOP (1ckf)CATH (1ckf)Homo sapiens
1ckg, downloadSCOP (1ckg)CATH (1ckg)Homo sapiens
1ckh, downloadSCOP (1ckh)CATH (1ckh)Homo sapiens
1d6p, downloadSCOP (1d6p)CATH (1d6p)Homo sapiens
1d6q, downloadSCOP (1d6q)CATH (1d6q)Homo sapiens
1di3, downloadSCOP (1di3)CATH (1di3)Homo sapiens
1di4, downloadSCOP (1di4)CATH (1di4)Homo sapiens
1di5, downloadSCOP (1di5)CATH (1di5)Homo sapiens
1eq4, downloadSCOP (1eq4)CATH (1eq4)Homo sapiens
1eq5, downloadSCOP (1eq5)CATH (1eq5)Homo sapiens
1eqe, downloadSCOP (1eqe)CATH (1eqe)Homo sapiens
1gay, downloadSCOP (1gay)CATH (1gay)Homo sapiens
1gaz, downloadSCOP (1gaz)CATH (1gaz)Homo sapiens
1gb0, downloadSCOP (1gb0)CATH (1gb0)Homo sapiens
1gb2, downloadSCOP (1gb2)CATH (1gb2)Homo sapiens
1gb3, downloadSCOP (1gb3)CATH (1gb3)Homo sapiens
1gb5, downloadSCOP (1gb5)CATH (1gb5)Homo sapiens
1gb6, downloadSCOP (1gb6)CATH (1gb6)Homo sapiens
1gb7, downloadSCOP (1gb7)CATH (1gb7)Homo sapiens
1gb8, downloadSCOP (1gb8)CATH (1gb8)Homo sapiens
1gb9, downloadSCOP (1gb9)CATH (1gb9)Homo sapiens
1gbo, downloadSCOP (1gbo)CATH (1gbo)Homo sapiens
1gbw, downloadSCOP (1gbw)CATH (1gbw)Homo sapiens
1gbx, downloadSCOP (1gbx)CATH (1gbx)Homo sapiens
1gby, downloadSCOP (1gby)CATH (1gby)Homo sapiens
1gbz, downloadSCOP (1gbz)CATH (1gbz)Homo sapiens
1gdw, downloadSCOP (1gdw)CATH (1gdw)Homo sapiens
1gdx, downloadSCOP (1gdx)CATH (1gdx)Homo sapiens
1ge0, downloadSCOP (1ge0)CATH (1ge0)Homo sapiens
1ge1, downloadSCOP (1ge1)CATH (1ge1)Homo sapiens
1ge2, downloadSCOP (1ge2)CATH (1ge2)Homo sapiens
1ge3, downloadSCOP (1ge3)CATH (1ge3)Homo sapiens
1ge4, downloadSCOP (1ge4)CATH (1ge4)Homo sapiens
1gev, downloadSCOP (1gev)CATH (1gev)Homo sapiens
1gez, downloadSCOP (1gez)CATH (1gez)Homo sapiens
1gf0, downloadSCOP (1gf0)CATH (1gf0)Homo sapiens
1gf3, downloadSCOP (1gf3)CATH (1gf3)Homo sapiens
1gf4, downloadSCOP (1gf4)CATH (1gf4)Homo sapiens
1gf5, downloadSCOP (1gf5)CATH (1gf5)Homo sapiens
1gf6, downloadSCOP (1gf6)CATH (1gf6)Homo sapiens
1gf7, downloadSCOP (1gf7)CATH (1gf7)Homo sapiens
1gf8, downloadSCOP (1gf8)CATH (1gf8)Homo sapiens
1gf9, downloadSCOP (1gf9)CATH (1gf9)Homo sapiens
1gfa, downloadSCOP (1gfa)CATH (1gfa)Homo sapiens
1gfe, downloadSCOP (1gfe)CATH (1gfe)Homo sapiens
1gfg, downloadSCOP (1gfg)CATH (1gfg)Homo sapiens
1gfh, downloadSCOP (1gfh)CATH (1gfh)Homo sapiens
1gfj, downloadSCOP (1gfj)CATH (1gfj)Homo sapiens
1gfk, downloadSCOP (1gfk)CATH (1gfk)Homo sapiens
1gfr, downloadSCOP (1gfr)CATH (1gfr)Homo sapiens
1gft, downloadSCOP (1gft)CATH (1gft)Homo sapiens
1gfu, downloadSCOP (1gfu)CATH (1gfu)Homo sapiens
1gfv, downloadSCOP (1gfv)CATH (1gfv)Homo sapiens
1hnl, downloadSCOP (1hnl)CATH (1hnl)Homo sapiens
1i22, downloadSCOP (1i22)CATH (1i22)Homo sapiens
1inu, downloadSCOP (1inu)CATH (1inu)Homo sapiens
1ioc, downloadSCOP (1ioc)CATH (1ioc)Homo sapiens
1ip1, downloadSCOP (1ip1)CATH (1ip1)Homo sapiens
1ip2, downloadSCOP (1ip2)CATH (1ip2)Homo sapiens
1ip3, downloadSCOP (1ip3)CATH (1ip3)Homo sapiens
1ip4, downloadSCOP (1ip4)CATH (1ip4)Homo sapiens
1ip5, downloadSCOP (1ip5)CATH (1ip5)Homo sapiens
1ip6, downloadSCOP (1ip6)CATH (1ip6)Homo sapiens
1ip7, downloadSCOP (1ip7)CATH (1ip7)Homo sapiens
1iwt, downloadSCOP (1iwt)CATH (1iwt)Homo sapiens
1iwu, downloadSCOP (1iwu)CATH (1iwu)Homo sapiens
1iwv, downloadSCOP (1iwv)CATH (1iwv)Homo sapiens
1iww, downloadSCOP (1iww)CATH (1iww)Homo sapiens
1iwx, downloadSCOP (1iwx)CATH (1iwx)Homo sapiens
1iwy, downloadSCOP (1iwy)CATH (1iwy)Homo sapiens
1iwz, downloadSCOP (1iwz)CATH (1iwz)Homo sapiens
1ix0, downloadSCOP (1ix0)CATH (1ix0)Homo sapiens
1iy3, downloadSCOP (1iy3)CATH (1iy3)Homo sapiens
1iy4, downloadSCOP (1iy4)CATH (1iy4)Homo sapiens
1jka, downloadSCOP (1jka)CATH (1jka)Homo sapiens
1jkb, downloadSCOP (1jkb)CATH (1jkb)Homo sapiens
1jkc, downloadSCOP (1jkc)CATH (1jkc)Homo sapiens
1jkd, downloadSCOP (1jkd)CATH (1jkd)Homo sapiens
1jsf, downloadSCOP (1jsf)CATH (1jsf)Homo sapiens
1jwr, downloadSCOP (1jwr)CATH (1jwr)Homo sapiens
1laa, downloadSCOP (1laa)CATH (1laa)Homo sapiens
1lhh, downloadSCOP (1lhh)CATH (1lhh)Homo sapiens
1lhi, downloadSCOP (1lhi)CATH (1lhi)Homo sapiens
1lhj, downloadSCOP (1lhj)CATH (1lhj)Homo sapiens
1lhk, downloadSCOP (1lhk)CATH (1lhk)Homo sapiens
1lhl, downloadSCOP (1lhl)CATH (1lhl)Homo sapiens
1lhm, downloadSCOP (1lhm)CATH (1lhm)Homo sapiens
1lmt, downloadSCOP (1lmt)CATH (1lmt)Homo sapiens
1loz, downloadSCOP (1loz)CATH (1loz)Homo sapiens
1lyy, downloadSCOP (1lyy)CATH (1lyy)Homo sapiens
1lz1, downloadSCOP (1lz1)CATH (1lz1)Homo sapiens
1lz4, downloadSCOP (1lz4)CATH (1lz4)Homo sapiens
1lz5, downloadSCOP (1lz5)CATH (1lz5)Homo sapiens
1lz6, downloadSCOP (1lz6)CATH (1lz6)Homo sapiens
1lzr, downloadSCOP (1lzr)CATH (1lzr)Homo sapiens
1lzs, downloadSCOP (1lzs)CATH (1lzs)Homo sapiens
1op9, downloadSCOP (1op9)CATH (1op9)Homo sapiens
1oua, downloadSCOP (1oua)CATH (1oua)Homo sapiens
1oub, downloadSCOP (1oub)CATH (1oub)Homo sapiens
1ouc, downloadSCOP (1ouc)CATH (1ouc)Homo sapiens
1oud, downloadSCOP (1oud)CATH (1oud)Homo sapiens
1oue, downloadSCOP (1oue)CATH (1oue)Homo sapiens
1ouf, downloadSCOP (1ouf)CATH (1ouf)Homo sapiens
1oug, downloadSCOP (1oug)CATH (1oug)Homo sapiens
1ouh, downloadSCOP (1ouh)CATH (1ouh)Homo sapiens
1oui, downloadSCOP (1oui)CATH (1oui)Homo sapiens
1ouj, downloadSCOP (1ouj)CATH (1ouj)Homo sapiens
1re2, downloadSCOP (1re2)CATH (1re2)Homo sapiens
1rem, downloadSCOP (1rem)CATH (1rem)Homo sapiens
1rex, downloadSCOP (1rex)CATH (1rex)Homo sapiens
1rey, downloadSCOP (1rey)CATH (1rey)Homo sapiens
1rez, downloadSCOP (1rez)CATH (1rez)Homo sapiens
1tay, downloadSCOP (1tay)CATH (1tay)Homo sapiens
1tby, downloadSCOP (1tby)CATH (1tby)Homo sapiens
1tcy, downloadSCOP (1tcy)CATH (1tcy)Homo sapiens
1tdy, downloadSCOP (1tdy)CATH (1tdy)Homo sapiens
1ubz, downloadSCOP (1ubz)CATH (1ubz)Homo sapiens
1w08, downloadSCOP (1w08)CATH (1w08)Homo sapiens
1wqm, downloadSCOP (1wqm)CATH (1wqm)Homo sapiens
1wqn, downloadSCOP (1wqn)CATH (1wqn)Homo sapiens
1wqo, downloadSCOP (1wqo)CATH (1wqo)Homo sapiens
1wqp, downloadSCOP (1wqp)CATH (1wqp)Homo sapiens
1wqq, downloadSCOP (1wqq)CATH (1wqq)Homo sapiens
1wqr, downloadSCOP (1wqr)CATH (1wqr)Homo sapiens
1yam, downloadSCOP (1yam)CATH (1yam)Homo sapiens
1yan, downloadSCOP (1yan)CATH (1yan)Homo sapiens
1yao, downloadSCOP (1yao)CATH (1yao)Homo sapiens
1yap, downloadSCOP (1yap)CATH (1yap)Homo sapiens
1yaq, downloadSCOP (1yaq)CATH (1yaq)Homo sapiens
207l, downloadSCOP (207l)CATH (207l)Homo sapiens
208l, downloadSCOP (208l)CATH (208l)Homo sapiens
2bqa, downloadSCOP (2bqa)CATH (2bqa)Homo sapiens
2bqb, downloadSCOP (2bqb)CATH (2bqb)Homo sapiens
2bqc, downloadSCOP (2bqc)CATH (2bqc)Homo sapiens
2bqd, downloadSCOP (2bqd)CATH (2bqd)Homo sapiens
2bqe, downloadSCOP (2bqe)CATH (2bqe)Homo sapiens
2bqf, downloadSCOP (2bqf)CATH (2bqf)Homo sapiens
2bqg, downloadSCOP (2bqg)CATH (2bqg)Homo sapiens
2bqh, downloadSCOP (2bqh)CATH (2bqh)Homo sapiens
2bqi, downloadSCOP (2bqi)CATH (2bqi)Homo sapiens
2bqj, downloadSCOP (2bqj)CATH (2bqj)Homo sapiens
2bqk, downloadSCOP (2bqk)CATH (2bqk)Homo sapiens
2bql, downloadSCOP (2bql)CATH (2bql)Homo sapiens
2bqm, downloadSCOP (2bqm)CATH (2bqm)Homo sapiens
2bqn, downloadSCOP (2bqn)CATH (2bqn)Homo sapiens
2bqo, downloadSCOP (2bqo)CATH (2bqo)Homo sapiens
2hea, downloadSCOP (2hea)CATH (2hea)Homo sapiens
2heb, downloadSCOP (2heb)CATH (2heb)Homo sapiens
2hec, downloadSCOP (2hec)CATH (2hec)Homo sapiens
2hed, downloadSCOP (2hed)CATH (2hed)Homo sapiens
2hee, downloadSCOP (2hee)CATH (2hee)Homo sapiens
2hef, downloadSCOP (2hef)CATH (2hef)Homo sapiens
2lhm, downloadSCOP (2lhm)CATH (2lhm)Homo sapiens
2mea, downloadSCOP (2mea)CATH (2mea)Homo sapiens
2meb, downloadSCOP (2meb)CATH (2meb)Homo sapiens
2mec, downloadSCOP (2mec)CATH (2mec)Homo sapiens
2med, downloadSCOP (2med)CATH (2med)Homo sapiens
2mee, downloadSCOP (2mee)CATH (2mee)Homo sapiens
2mef, downloadSCOP (2mef)CATH (2mef)Homo sapiens
2meg, downloadSCOP (2meg)CATH (2meg)Homo sapiens
2meh, downloadSCOP (2meh)CATH (2meh)Homo sapiens
2mei, downloadSCOP (2mei)CATH (2mei)Homo sapiens
2nwd, downloadSCOP (2nwd)CATH (2nwd)Homo sapiens
2zij, downloadSCOP (2zij)CATH (2zij)Homo sapiens
2zik, downloadSCOP (2zik)CATH (2zik)Homo sapiens
2zil, downloadSCOP (2zil)CATH (2zil)Homo sapiens
2zwb, downloadSCOP (2zwb)CATH (2zwb)Homo sapiens
3eba, downloadSCOP (3eba)CATH (3eba)Homo sapiens
3fe0, downloadSCOP (3fe0)CATH (3fe0)Homo sapiens
3lhm, downloadSCOP (3lhm)CATH (3lhm)Homo sapiens
3ln2, downloadSCOP (3ln2)CATH (3ln2)Homo sapiens
3sn6, downloadSCOP (3sn6)CATH (3sn6)Homo sapiens
135l, downloadSCOP (135l)CATH (135l)Meleagris gallopavo
1dzb, downloadSCOP (1dzb)CATH (1dzb)Meleagris gallopavo
1jef, downloadSCOP (1jef)CATH (1jef)Meleagris gallopavo
1jse, downloadSCOP (1jse)CATH (1jse)Meleagris gallopavo
1jtp, downloadSCOP (1jtp)CATH (1jtp)Meleagris gallopavo
1ljn, downloadSCOP (1ljn)CATH (1ljn)Meleagris gallopavo
1lzy, downloadSCOP (1lzy)CATH (1lzy)Meleagris gallopavo
1tew, downloadSCOP (1tew)CATH (1tew)Meleagris gallopavo
1uac, downloadSCOP (1uac)CATH (1uac)Meleagris gallopavo
1xft, downloadSCOP (1xft)CATH (1xft)Meleagris gallopavo
2lz2, downloadSCOP (2lz2)CATH (2lz2)Meleagris gallopavo
3lz2, downloadSCOP (3lz2)CATH (3lz2)Meleagris gallopavo
3ab6, downloadSCOP (3ab6)CATH (3ab6)Meretrix lusoria
3ayq, downloadSCOP (3ayq)CATH (3ayq)Meretrix lusoria
1ivm, downloadSCOP (1ivm)CATH (1ivm)Mus musculus
2fbd, downloadSCOP (2fbd)CATH (2fbd)Musca domestica
2h5z, downloadSCOP (2h5z)CATH (2h5z)Musca domestica
3cb7, downloadSCOP (3cb7)CATH (3cb7)Musca domestica
2x8r, downloadSCOP (2x8r)CATH (2x8r)Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100)
1fbi, downloadSCOP (1fbi)CATH (1fbi)Numida meleagris
1hhl, downloadSCOP (1hhl)CATH (1hhl)Numida meleagris
1bb6, downloadSCOP (1bb6)CATH (1bb6)Oncorhynchus mykiss
1bb7, downloadSCOP (1bb7)CATH (1bb7)Oncorhynchus mykiss
1lmc, downloadSCOP (1lmc)CATH (1lmc)Oncorhynchus mykiss
1lmn, downloadSCOP (1lmn)CATH (1lmn)Oncorhynchus mykiss
1lmo, downloadSCOP (1lmo)CATH (1lmo)Oncorhynchus mykiss
1lmp, downloadSCOP (1lmp)CATH (1lmp)Oncorhynchus mykiss
1lmq, downloadSCOP (1lmq)CATH (1lmq)Oncorhynchus mykiss
1d6p, downloadSCOP (1d6p)CATH (1d6p)Pan paniscus
1d6q, downloadSCOP (1d6q)CATH (1d6q)Pan paniscus
1lmt, downloadSCOP (1lmt)CATH (1lmt)Pan paniscus
1lzr, downloadSCOP (1lzr)CATH (1lzr)Pan paniscus
1lzs, downloadSCOP (1lzs)CATH (1lzs)Pan paniscus
1re2, downloadSCOP (1re2)CATH (1re2)Pan paniscus
1rem, downloadSCOP (1rem)CATH (1rem)Pan paniscus
1rey, downloadSCOP (1rey)CATH (1rey)Pan paniscus
1rez, downloadSCOP (1rez)CATH (1rez)Pan paniscus
1ubz, downloadSCOP (1ubz)CATH (1ubz)Pan paniscus
1w08, downloadSCOP (1w08)CATH (1w08)Pan paniscus
207l, downloadSCOP (207l)CATH (207l)Pan paniscus
208l, downloadSCOP (208l)CATH (208l)Pan paniscus
1d6p, downloadSCOP (1d6p)CATH (1d6p)Pan troglodytes
1d6q, downloadSCOP (1d6q)CATH (1d6q)Pan troglodytes
1lmt, downloadSCOP (1lmt)CATH (1lmt)Pan troglodytes
1lzr, downloadSCOP (1lzr)CATH (1lzr)Pan troglodytes
1lzs, downloadSCOP (1lzs)CATH (1lzs)Pan troglodytes
1re2, downloadSCOP (1re2)CATH (1re2)Pan troglodytes
1rem, downloadSCOP (1rem)CATH (1rem)Pan troglodytes
1rey, downloadSCOP (1rey)CATH (1rey)Pan troglodytes
1rez, downloadSCOP (1rez)CATH (1rez)Pan troglodytes
1ubz, downloadSCOP (1ubz)CATH (1ubz)Pan troglodytes
1w08, downloadSCOP (1w08)CATH (1w08)Pan troglodytes
207l, downloadSCOP (207l)CATH (207l)Pan troglodytes
208l, downloadSCOP (208l)CATH (208l)Pan troglodytes
2gv0, downloadSCOP (2gv0)CATH (2gv0)Pelodiscus sinensis
1ghl, downloadSCOP (1ghl)CATH (1ghl)Phasianus colchicus colchicus
3mgw, downloadSCOP (3mgw)CATH (3mgw)Salmo salar
1h09, downloadSCOP (1h09)CATH (1h09)Streptococcus phage Cp-1
1oba, downloadSCOP (1oba)CATH (1oba)Streptococcus phage Cp-1
2ixu, downloadSCOP (2ixu)CATH (2ixu)Streptococcus phage Cp-1
2ixv, downloadSCOP (2ixv)CATH (2ixv)Streptococcus phage Cp-1
2j8f, downloadSCOP (2j8f)CATH (2j8f)Streptococcus phage Cp-1
2j8g, downloadSCOP (2j8g)CATH (2j8g)Streptococcus phage Cp-1
2ww5, downloadSCOP (2ww5)CATH (2ww5)Streptococcus pneumoniae
2wwc, downloadSCOP (2wwc)CATH (2wwc)Streptococcus pneumoniae
2wwd, downloadSCOP (2wwd)CATH (2wwd)Streptococcus pneumoniae
1jfx, downloadSCOP (1jfx)CATH (1jfx)Streptomyces globisporus
1jug, downloadSCOP (1jug)CATH (1jug)Tachyglossus aculeatus aculeatus
2dqa, downloadSCOP (2dqa)CATH (2dqa)Venerupis philippinarum
4arj, downloadSCOP (4arj)CATH (4arj)Yersinia pestis
4epi, downloadSCOP (4epi)CATH (4epi)Yersinia pestis
4exm, downloadSCOP (4exm)CATH (4exm)Yersinia pestis

MOLECULAR WEIGHT MOLECULAR WEIGHT MAXIMUM ORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE
10000-Heliothis virescens-gel filtration171046
1100013000unidentified phage-Archibald sedimentation equilibrium method171073
1400014850Bos taurus-4 isoforms, ion spray mass spectometry171104
1400016000Homo sapiens-sedimentation velocity, short-column sedimentation equilibrium, amino acid analysis171088
14000-Ornithodoros moubata-MALDI-TOF mass spectrometry171097
14000-Gallus gallus--709169
14120-Gallus gallus-MADI-TOF708795
14300-Oryctolagus cuniculus-gel filtration171055
14310-Gallus gallus-FT-ICR mass spectroscopy171089
14400-Equus caballus-gel filtration171074
14600-Gallus gallus--709764
14660-Equus caballus-ESI mass spectroscopy171109
1500017000Homo sapiens-analytical ultracentrifugation171085
15000-Enterobacteria phage T4-gel filtration171048
15000-Bos taurus-gel filtration171049
15000-Papio cynocephalus-amino acid analysis171078
15000-Fenneropenaeus merguiensis-12% SDS-PAGE709875
15400-Nilssonia gangetica-sedimentation and diffusion coefficient values, low speed sedimentation, Archibald's method, amino, acid composition171061
17600-unidentified phage-sedimentation analysis, sequential analysis171073
17900-Enterobacteria phage lambda-sedimentation equilibrium data, sedimentation and diffusion coefficient171087
18500-Saccharopolyspora erythraea-ultracentrifugation171059
18600-unidentified phage-amino acid composition171073
19000-unidentified phage-low speed sedimentation, Archibald's method171073
20870-Ruditapes philippinarum-the ORF encoded a protein of 185 amino acid residues with a calculated molecular mass of 20.87 kDa708229
23200-Ceratitis capitata-gel filtration171065
24000-Pseudomonas aeruginosa-gel filtration171058
24000-Medicago sativa-CHIT24, gel filtration171096
25000-Brassica sp.-gel filtration171079
28800-Pseudomonas phage phiKZQ8SD18calculated molecular mass683684
29000-Ficus sp.-ultracentrifugation171086
30000-Pseudomonas aeruginosa-FII, gel filtration171095
30000-Streptococcus pneumoniae--706988
36000-Medicago sativa-CHIT36, gel filtration171096
44000-Clostridium acetobutylicum-gel filtration171101
60000-Pseudomonas aeruginosa-FI, gel filtration171095
200000-Enterobacteria phage P22-gel filtration171077
250000-Carica papaya-ultracentrifugation171080
additional information-unidentified phage--171073

SUBUNITS ORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE
?Streptococcus pneumoniae-x * 55000, SDS-PAGE171051
?Canis lupus familiaris-x * 14500, SDS-PAGE171098
?Clostridium phage phi3626-x * 38800, SDS-PAGE654265
?Lactococcus lactisQ8KKF9x * 57100, sequence calculation656731
?Enterobacteria phage phiKMV-x * 20884, SELDI-TOF664563
?Crassostrea virginica-x * 17771.5, two potential forms of enzyme: 17771.5 Da and 17861 Da, MALDI-MS; x * 17861, MALDI-MS; x * 18400, SDS-PAGE664651
?Bufo andrewsi-x * 14745, calculated from sequence; x * 15000, SDS-PAGE664671
?Helicoverpa zea-x * 14400, SDS-PAGE665818
?Bacillus sp.-x * 15800, SDS-PAGE; x * 16464, matrix-assisted laser desorption ionization time-of-flight mass spectrometry677778
?Larimichthys crocea-x * 21300, calculated from sequence677863
?Saxidomus purpuratus-x * 12000, SDS-PAGE679932
?Liolophura japonica, Micrococcus luteus, Omphalius pfeifferi-x * 12000, SDS-PAGE679934
?Bacillus sp.-x * 15800, SDS-PAGE679957
?Chlamys farreriQ075V3x * 20010, calculated from sequence681964
?Helicoverpa armigeraQ19R28x * 15600, calculated and SDS-PAGE of recombinant protein695906
?unidentified phageQ859R8x * 33000, SDS-PAGE, x * 33141, calculated696020
?Homo sapiens-x * 14672, calculated696869
?Anopheles gambiaeA4ZWD2, Q7QHB9x * 14860, calculated, mature protein; x * 15880, calculated, mature protein698287
?Musca domesticaB3GQR5x * 13800, calculated699304
?Rhodnius prolixusA9LN31, A9LN32x * 15100, calculated; x * 15800, calculated699392
?Penaeus monodonQ8IT75x * 16320, calculated, x * 16000, SDS-PAGE700107
?Homo sapiensQ86SG7x * 21508, sequence calculation718120
?Homo sapiens-x * 14679.14, mass spectrometry718276
dimerPseudomonas aeruginosa-2 * 30000, SDS-PAGE171095
dimerGallus gallus-formation of covalent bonds between lysozyme molecules by zero-length cross-linking. Approximately one-third of the total lysozyme becomes cross-linked. The enzymatic activity of cross-linked lysozyme dimer is the same as monomer. The activity of lysozyme dimer remains constant up to 10 min at 80°C. Lysozyme possess a compact structure in the dimer form680207
monomerHeliothis virescens-1 * 16000, SDS-PAGE171046
monomerPseudomonas aeruginosa-FII, 1 * 32000, SDS-PAGE171095
monomerMedicago sativa-CHIT24, 1 * 24000, SDS-PAGE; CHIT36, SDS-PAGE171096
monomerClostridium acetobutylicum-1 * 41000, SDS-PAGE171101
monomerBos taurus-4 isoforms, 1 * 14100-15000, SDS-PAGE171104
monomerEnterobacteria phage T4-1 * 18700718395
additional informationGallus gallus-quantitative characterization of the kinetic mechanism of tertiary and secondary structural evolution of hen egg white lysozyme at the early stages of its fibrillation using the new 2D simulation-aided deep UV resonance Raman spectroscopy680380
additional informationMusca domestica-structure analysis of MdL1 and MdL2, overview. Residues S106-T107 delimit a polar pocket around E32, as catalytic acid/base, and N46 contributes to the positioning of D50, as catalytic nucleophile717509
additional informationSalmo salarA6PZ97structure homology modeling, overview717510
additional informationGallus gallus-secondary structure of lysozyme, free and bound to gold nanorods, no significant change in the secondary structure occurs upon binding, overview717672
additional informationHomo sapiens-peptide mass fingerprinting of recombinant enzymes, overview718276

POSTTRANSLATIONAL MODIFICATION ORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE
proteolytic modificationAnopheles gambiaeA4ZWD2, Q7QHB9cleavage of signal peptide between amino acids 20 and 21; cleavage of signal peptide between amino acids 21 and 22698287
additional informationAnopheles gambiaeA4ZWD2, Q7QHB9sequence contains no predicted glycosylation site; sequence contains one potential N-glycosylation site at postion 7 of the mature peptide698287
glycoproteinGallus gallus-engineered glycosylation sites at postition 19 and 49171094
additional informationGallus gallus-modified with methoxypolyethylene glycol-p-nitrophenyl carbonate (mPEG-pNP, MW 5000)708795
proteolytic modificationHelicoverpa zea-signal peptide of 20 amino acids at the N-terminus665818
additional informationMusca domesticaB3GQR5sequence contains eight cysteines within mature peptides forming 4 pairs of disulfide bridges necessary for enzymatic activity699304

Crystallization/COMMENTARY ORGANISM UNIPROT ACCESSION NO. LITERATURE
modeling of complex with GlcNAcbeta(1-4)GlcNAcbeta(1-4)GlcNAcbeta(1-4)GlcNAcbeta(1-4)GlcNAcbeta(1-4)GlcNAcbetaAnser anser-698655
hanging drop vapor diffusion methodBacillus anthracis-708007
recombinant bovine stomach lysozyme 2, to 1.5 A resolution. Space group P212121. Stability may be due to negatively charged surfaces, a shortened loop and slat bridgesBos taurusQ06283697903
crystal structure of mutant N44Q/N47Q/N49Q/N68Q/N103Q is substantially identical to that of the wild type, and the substitutions of Asn to Gln are appropriate for the folding and structural analyses of this proteinCanis lupus familiaris-701125
-Enterobacteria phage T4-171042, 171073
the crystal structure of the switch mutant L20/R63A liganded to both methyl- and ethylguanidinium ions is determined at resolutions of 1.7 A and 1.8 A, respectivelyEnterobacteria phage T4-682730
comparison of native and A-statesEquus caballus-171091
phage T4 induced: study of structural basis of thermal stabilityEscherichia coli-171042
hanging drop vapor diffusion methodGadus morhua-708057
-Gallus gallus-171092, 171099
asparagine and glutamine side-chain conformation in solution and crystal: a comparison for hen egg-white lysozyme using residual dipolar couplingsGallus gallus-665757
atomic and molecular displacementsGallus gallus-171043
crystallization and X-ray characterization of chemically glycosylated hen egg-white lysozymeGallus gallus-663529
crystallization conditionsGallus gallus-171039
crystallization data in complex with membrane bound lysozyme inhibitor of C-type lysozyme MliC. The invariant loop of MliC plays a crucial role in the inhibition by its insertion to the active site cleft of the lysozyme, where the loop forms hydrogen and ionic bonds with the catalytic residuesGallus gallus-696021
crystallographic studies of denaturation and renaturationGallus gallus-171062, 171063
determinatipon of crystallization phase diagrams at pH 2.5, pH 6.0, and pH 7.5. At pH values below 4.5, the border between the metastable region and the nucleation region shifts to the lower precipitant concentration in the phase diagramm and at pH values above 4.5, the border shifts to higher precipitant concentrations. The qualities of crystals at different pH values are more or less equivalentGallus gallus-699858
hanging drop methodGallus gallus-710026
hanging drop method and nanotemplate crystallization method. Crystals grown by the nanostructured template method appear radiation-resistantGallus gallus-663508
hanging drop method, crystals of native enzyme and enzyme in complex with various alcohols (ethanol, 1-butanol, 1-pentanol, 2-propanol or TFE). Although the alcohols have very little effect on the conformation of the overall protein structure, they profoundly affect protein hydration and disorder of the bound water. Increasing order of hydrophobicity of alcohols is directly proportional to the higher number of weakly bound waters in the proteinGallus gallus-663498
hexagonal crystal crystallize from a saturated sodium nitrate solution at pH 8.4, crystals belong to space group P6(1)22, with unit-cell parameters a = b = 85.64, c = 67.93 A. 1.46 A resolutionGallus gallus-663510
kinetics and thermodynamics of lysozyme precipitation in ammonium sulfate solutions at pH 4 and 8 and room temperature. If sufficient time is allowed, microcrystals develop following an induction period after initial lysozyme precipitation, even up to ionic strengths of 8 M and at acidic pH, where lysozyme is refractory to crystallization in ammonium sulfateGallus gallus-678844
measurement of lysozyme solubility in aqueous solutions as a function of NaCl, KCl, and NH4Cl concentrations at 25°C and pH 4.5. Simple model for the crystalline phase based on salt partitioning between solution and the hydrated protein crystalGallus gallus-698462
membrane crystallization of lysozyme under forced solution flowGallus gallus-665993
mutants K33A and K33N. The side chain of K33 in wild-type hydrogen bonds with N37 involved in the substrate-binding region. Orientation of N37 differs in mutants K33A and K33NGallus gallus-698654
pure enzyme, hanging drop vapour diffusion method, 50 or 150 mg/ml enzyme in 0.1 M sodium acetate, pH 4.5, sodium phosphate, pH 6.5, or Tris-HCl, pH 8.5, mixing of 0.0015 ml of protein solution and 0.0015 ml of reservoir solution, equilibration against 0.5 ml of reservoir solutiom, 20°C, crystallization method evaluation using Gly, Ser, Asp, Glu, Arg, ornithine, Lys and glycine ethyl ester as precipitants at pH 4.5, 6.5 and 8.5, X-ray diffraction structure determination and analysis at 1.7-1.8 A resolutionGallus gallus-717036
-Homo sapiens-171066, 171100
purified recombinant mutant R101D/R115H, 7 mg/ml protein in 10 mM potassium phosphate, pH 6.0, 100 mM NaCl, is mixed with crystallization solution containing 20 mM sodium acetate, pH 4.3, and 1.25 M NaCl, 18°C, 3-4 days, X-ray diffraction structure determination and analysis at 2.04 A resolution, molecular replacement and modelingHomo sapiens-718273
-Meleagris gallopavo-171082
purified recombinant MdL2, sitting drop vapour diffusion method, 18°C, precipitant solution containing 28% isopropanol, 21% PEG 4000, and 0.115 M sodium citrate pH 4.2, addition of 0.2 M ammonium acetate, 30% 2-methyl-2,2-pentanediol, 0.1 M sodium citrate, pH 5.6, X-ray diffraction structure determination and analysis at 1.9 A resolution, modelingMusca domestica-717509
sitting-drop vapour-diffusion method in the presence of ammonium sulfate or PEG/2-propanol as the precipitant. X-ray diffraction data are collected to a maximum resolution of 1.9 A using synchrotron radiation. The lysozyme 1 crystals belong to the monoclinic space group P2(1), unit-cell parameters a = 36.52, b = 79.44, c = 45.20 A, beta = 102.97°; sitting-drop vapour-diffusion method in the presence of ammonium sulfate or PEG/2-propanol as the precipitant. X-ray diffraction data are collected to a maximum resolution of 1.9 A using synchrotron radiation. The lysozyme 2 crystals belong to the orthorhombic space group P2(1)2(1)2, unit-cell parameters are a = 73.90, b = 96.40, c = 33.27 AMusca domesticaQ7YT17677356
vapour-diffusion sitting-drop method, structure of lysozyme c in native form and complexed form with (N-acetylglucosamine)3Musca domestica-681655
-Nilssonia gangetica-171061
1.9 A resolution, space group P212121. Positions of P104 in the substrate subsite A and other amino acids in the subsites E and F differ from those of hen egg white, while the overall stuctures are very similarPelodiscus sinensisQ7LZQ1698657
the x-ray structure of the lytic transglycosylase gp144 is determined to 2.5 A resolution, in complex with chitotetraose, (N-acetylglucosamine)4, to 2.6 A resolutionPseudomonas phage phiKZQ8SD18683684
vapor diffusion hanging drop method, crystal structure of the enzyme complexed with a trimer of N-acetylglucosamine to 1.6 A resolutionRuditapes philippinarum-680812
-Saccharopolyspora erythraea-171059
purified enzyme, hanging drop vapour diffusion method, 0.001 ml of 8 mg/ml protein in 150mM NaCl and 50 mM HEPES, pH 7.25, is mixed with 0.001 ml of reservoir solutions containing 43-45% ammonium sulfate, 0.01 M cobalt chloride, and 0.1 M MES, pH 6.25-6.5, 22°C, 3 weeks, X-ray diffraction structure determination and analysis at 1.75 A resolutionSalmo salarA6PZ97717510
hangingdrop and sitting-drop vapour-diffusion methodsStreptococcus pneumoniae-706988
-unidentified phage-171073

pH STABILITYpH STABILITY MAXIMUM ORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE
213Crassostrea virginica-30 min, stable664651
2.86.4Liolophura japonica-stable pH-range679934
310Rhea americana, Struthio camelus-37°C, 4 h, stable664365
3.5-Ceratitis capitata-stability at acidic pH, stable for weeks at 4°C171065
4.85.6Micrococcus luteus-stable pH-range679934
4.86Omphalius pfeifferi-stable pH-range679934
4.86.8Saxidomus purpuratus-stable pH-range679932
68Pseudomonas aeruginosa-stable in presence of 0.01% bovine serum albumin171058
6.5-Pseudomonas aeruginosa-stable at high enzyme concentrations, for at least 2 months at 4°C171058
8.7-Ceratitis capitata-lability at alkaline pH171065
12.2-Gallus gallus-lysozyme sponaneously forms soluble oligomers, which are later stabilized by intermolecular disulfide bonds696471

TEMPERATURE STABILITYTEMPERATURE STABILITY MAXIMUM ORGANISM UNIPROT ACCESSION NO. COMMENTARYLITERATURE
2030Rhea americana, Struthio camelus-10 min, stable664365
2070Bos taurus-unaffected, 10 min, pH 5.0171049
2090Saxidomus purpuratus-stable temperature-range679932
20-Bufo andrewsi-30 min, about 10% loss of activity664671
20-Xanthomonas phage Xop411A1BPG910 min, 3% loss of activity682650
25.3-Equus caballus-loss of 50% activity718376
30-Xanthomonas phage Xop411A1BPG910 min, 14% loss of activity682650
37-Pseudomonas aeruginosa-stable below171058
37-Homo sapiens-35% residual activity after 4 days, pH 4171088
40-Pseudomonas aeruginosa-unstable above171058
40-Enterobacteria phage P22-no loss of activity up to, 5 min171077
40-Rhea americana-10 min, about 20% loss of activity664365
40-Struthio camelus-10 min, about 15% loss of activity664365
40-Xanthomonas phage Xop411A1BPG910 min, 25% loss of activity682650
45-Enterobacteria phage T4-inactivation above, 10 min171052
45.3-Struthio camelus-melting temperature, mutant C4S/C18S/C29S/C60S697868
45.4-Streptococcus pneumoniae-thermal denaturation of the catalytic module698818
46.2-Struthio camelus-melting temperature, reduced wild-type697868
50-Pseudomonas aeruginosa-FI unaffected, 10 min171095
50-Struthio camelus-10 min, about 30% loss of activity664365
50-Xanthomonas phage Xop411A1BPG910 min, 30% loss of activity682650
51.1-Struthio camelus-melting temperature, mutant C4S/C60S697868
53-unidentified phage-50% inactivation at171073
54.3-Struthio camelus-melting temperature, mutant C18S/C29S697868
55-Struthio camelus-Tm-value for mutant enzyme E73S is 54.5°C680548
55-Xanthomonas phage Xop411A1BPG910 min, 66% loss of activity682650
57-Struthio camelus-Tm-value for mutant E73A is 57.4°C. Tm-value for mutant E73Q is 56.6°C680548
6070Struthio camelus-10 min, about 40% loss of activity664365
60-Pseudomonas aeruginosa-FII, unaffected, 10 min171095
60-Rhea americana-10 min, about 25% loss of activity664365
60-Homo sapiens-purified recombinant enzyme, 45 min, 95% activity remaining718276
60.6-Struthio camelus-melting temperature, wild-type697868
61-Struthio camelus-Tm-value for wild-type enzyme is 60.6°C680548
62.8-Bos taurusQ06283Tm value, pH 2.0697903
70-Enterobacteria phage T4-80% loss of activity after 10 min171053
70-Enterobacteria phage P22-90% loss of activity after 5 min171077
70-Rhea americana-10 min, about 30% loss of activity664365
70-Bufo andrewsi-30 min, about 15% loss of activity664671
76-Gallus gallus-mid-transition temperature is 76.3°C for S6K-lysozyme and 76.0°C for S7-lysozyme664351
77-Gallus gallus-mid-transition temperature of wild-type enzyme664351
80-Nilssonia gangetica-83% of activity of that at 25°C, more stable than hen lysozyme171061
80-Rhea americana-10 min, about 45% loss of activity664365
80-Struthio camelus-10 min, about 50% loss of activity664365
80-Bufo andrewsi-30 min, about 60% of maximal activity664671
80-Gallus gallus-the activity of lysozyme dimer remains constant up to 10 min680207
85-Gallus gallus-purified enzyme, pH 6.2, inactivation after 60 min717672
90-Rhea americana, Struthio camelus-about 60% loss of activity after 60 min, about 80% loss of activity after180 min664365
90-Salmo salar-3 h, 70% loss of activity679139
90-Amyda cartilaginea-180 min, about 35% loss of activity679342
90-Chelonia mydas-60 min, about 60% loss of activity679342
90-Pelodiscus sinensis-3 h, about 45% loss of activity, isoenzyme SSTL A; 90 min, about 70% loss of activity, isoenzyme SSTL B679342
90-Saxidomus purpuratus-30 min, 55% loss of activity679932
90-Liolophura japonica-30 min, 11% loss of activity679934
90-Micrococcus luteus-30 min, 69% loss of activity679934
90-Omphalius pfeifferi-30 min, 72% loss of activity679934
95-unidentified phageQ859R81 h, 38.6% residual activity in absence of 2-mercaptoethanol, 93.8% residual activity in presence of 2-mercaptoethanol696020
100-Heliothis virescens-stable for 60 min at pH 3171046
100-Enterobacteria phage phiKMV-2 h, 74% loss of activity664563
100-Homo sapiens-purified recombinant enzyme, 10 min, 50% activity remaining718276
120-Enterobacteria phage phiKMV-at 2 bar, 20 min, 79% loss of activity664563
additional information-Enterobacteria phage T4-mutant and wild-type, study of structural basis of thermal stability171042
additional information-Nilssonia gangetica-lysozyme more stable than hen lysozyme171061
additional information-Homo sapiens-human lysozyme more resistant to heat than chicken171075
additional information-Staphylococcus aureus--171081
additional information-Equus caballus-temperature induced transitions in equine lysozyme682754
additional information-Salmo salarA6PZ97unfolding and potential refolding analysis due to cold adaptation and heat treatment, differential scanning calorimetry. Recombinant SalG has a melting temperature of 36.8°C under thermal denaturation conditions and regains activity after returning to permissive (low) temperature. Rapid and irreversible inactivation takes place during heating at high enzyme concentration717510

GENERAL STABILITYORGANISM UNIPROT ACCESSION NO.LITERATURE
effects of freezing, thawing and freeze-drying are negligibleBos taurus-171049
lysozymes C unusually resistant to inactivation by pepsinBos taurus, Cervidae-171045
the apo-form of the enzyme is marginally stableEquus caballus-718376
the effects of sugars trehalose, maltose, and sucrose on the protein conformation are relatively weak, in agreement with the preferential hydration of lysozyme. Sugars seem to increase significantly the relaxation times of the protein. These effects are correlated to the fractional solvent accessibilities of lysozyme residues and further support the slaving of protein dynamicsGallus gallus-681598
the enzyme complexed to heparin shows a significantly reduced physical stability when stored at 37°C for 12 weeksGallus gallus-666541
at high concentrations or in presence of albumin, lyophilized or desalted without loss of activityOncorhynchus mykiss-171041
Na+ and Mg2+ exert a stabilizing effectunidentified phage-171073
lysozymes C unusually resistant to inactivation by pepsinOvis aries, Ruminantia-171045
additional informationunidentified phage-171073

ORGANIC SOLVENT ORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE
No entries in this field

OXIDATION STABILITY ORGANISM UNIPROT ACCESSION NO. LITERATURE
No entries in this field

STORAGE STABILITY ORGANISM UNIPROT ACCESSION NO. LITERATURE
4°C, storage for over a month without loss of activityEnterobacteria phage phiKMV-664563
no significant loss of the activity after 6 months of frozen storage for both wild-type and two-active site lysozymeHomo sapiens-677972
several months, at -20°C, 0.1% bovine serum albuminOryctolagus cuniculus-171055
additional informationCeratitis capitata-171065
several weeks at -20°CTriticum aestivum-171040
additional informationunidentified phage-171073

Purification/COMMENTARY ORGANISM UNIPROT ACCESSION NO. LITERATURE
-Amyda cartilaginea-679342
3 electrophoretic formsAnas platyrhynchos-171050
two step purification protocolAnopheles gambiaeQ17005708225
-Anser sp.-680229
-Bacillus sp.-677778, 679957
-Bos taurus-171045, 171049, 171093, 171104
-Brassica oleracea-680229
-Brassica sp.-171079
-Bufo andrewsi-664671
; serum, cartilageCanis lupus familiaris-171071
canine milk lysozyme exhibits charge heterogeneity after sample purification. Four Asn residues deamidate rapidly under mild conditions of pH 8.0 and 30°C. One Asn residue, which is stable in the native state, is labile to deamidation in the unfolded stateCanis lupus familiaris-701125
-Carica papaya-171080
-Ceratitis capitata-171065
-Cervidae-171045
-Chelonia mydas-679342, 682698
-Clostridium acetobutylicum-171101
recombinant Ply3626Clostridium phage phi3626-654265
-Crassostrea virginica-664651
rapid purification scheme in purifying both the wild-type and chimeric lysozymesEnterobacteria phage K11-680582
-Enterobacteria phage lambda-680229
host: E coliEnterobacteria phage lambda-171087
host: Salmonella typhimuriumEnterobacteria phage P22-171077
-Enterobacteria phage phiKMV-664563
-Enterobacteria phage T4-171048, 680229
recombinant extracellular enzyme from Hansenula polymorpha strain A16 culture supernatant by ammonium sulfate fractionation and ultrafiltrationEnterobacteria phage T4-718395
rapid purification scheme in purifying both the wild-type and chimeric lysozymesEnterobacteria phage T7-680582
-Equus caballus-171074
expression in Aspergillus nigerEquus caballus-171109
Ni21 affinity chromatographyEquus caballus-710467
-Ficus sp.-171086
-Gallus gallus-171057, 171068, 171111
efficient and inexpensive lysozyme purification from chicken egg white can be achieved by using polyethylene glycol-salt aqueous two-phase systemGallus gallus-666704
hydrophobic affinity ligand L-tryptophan immobilized magnetic poly(glycidyl methacrylate) [m-poly(GMA)] beads in monosize form (0.0016 mM in diameter) are used for the affinity purification of lysozyme from chicken egg white. The chemisorption processes can be the rate-limiting step in the adsorption process. After 10 adsorption-elution cycles, m-poly(GMA)-L-tryptophan beads can be used without significant loss in lysozyme adsorption capacityGallus gallus-681060
two serine-rich heptapeptides, Ser-Ser-Ser-Lys-Ser-Ser-Ser (S6K) and Ser-Ser-Ser-Ser-Ser-Ser-Ser (S7) are fused to the C-terminus of chicken lysozyme by genetic modification. The cDNAs of S6K-lysozyme and S7-lysozyme are inserted into the expression vector of Pichia pastoris and secreted in the yeast cultivation mediumGallus gallus-664351
-Heliothis virescens-171046
-Homo sapiens-171047, 171075, 171085, 171088, 677972
leukemia lysozymeHomo sapiens-171066
recombinant enzyme from Pichia pastoris strain GS115 by chitin affinity chromatography and gel filtration to homogeneityHomo sapiensQ86SG7718120
recombinant enzyme from transgenic cow milk, from which fat and casein has been removed for purification of the enzyme, by cation exchange chromatography and gel filtration to over 95% purityHomo sapiens-718276
recombinant AcmBLactococcus lactisQ8KKF9656731
recombinant enzymeLarimichthys crocea-677863
-Medicago sativa-171096
-Meleagris gallopavo-171082
-Musca domestica-171102, 681655
recombinant wild-type and mutant MdL2s from Pichia pastoris by ammonium sulfate fractionation, and cation exchange, for the sextuple mutant, or anion exchange, for the other mutants, chromatographyMusca domestica-717509
-Nilssonia gangetica-171061
C-terminal hexahistidine tail Lys44Oenococcus phage fOg44-680524
2 forms: I/II, c-typeOncorhynchus mykiss-171041
-Ornithodoros moubata-171097
-Oryctolagus cuniculus-171055, 171108
-Ovis aries-171045, 171093
-Papio cynocephalus-171078
-Pelodiscus sinensisQ7LZQ1698657
isoenzyme SSTL A; isoenzyme SSTL BPelodiscus sinensis-679342
recombinant protein, Escherichia coli inclusion bodiesPenaeus monodonQ8IT75700107
pyocinogenicPseudomonas aeruginosa-171058
using a HisTrap HP columnPseudomonas phage phiKZQ8SD18683684
-Rattus norvegicus-171054, 171067
CM-Sepharose column linked to an AEKTA-FPLC systemRuditapes philippinarum-708061
-Ruminantia-171045
-Saccharopolyspora erythraea-171059
-Saxidomus purpuratus-679932
-Staphylococcus aureus-171081
-Streptococcus pneumoniae-171051
the cell pellet is resuspended in 50 ml lysis buffer (20 mM Tris-HCl pH 8.0 and 300 mM sodium chloride) and lysed by sonication on ice. All subsequent purification steps are performed at 277 K. The lysate is centrifuged at 15 000g for 30 min. The supernatant is applied onto a 10 ml Ni2+-NTA affinity column (Qiagen) equilibrated with lysis buffer. Nonspecifically bound proteins are washed from the column using 200 ml lysis buffer containing 15 mM imidazole. The recombinant protein is then eluted from the column with 20 ml elution buffer containing 20 mM Tris-HCl pH 8.0, 300 mM sodium chloride and 400 mM imidazole. The protein is concentrated and buffer-exchanged to the final buffer (5 mM Tris-HCl pH 8.0 and 10 mM sodium chloride). The final purified protein concentration was about 50 mg/ml and the purity is determined by SDS-PAGE to be about 95%Streptococcus pneumoniae-706988
-Struthio camelus-680548
multiple electrophoretic formsTriticum aestivum-171040
-unidentified phage-171073
from lysates of phage grown on Thermus aquaticus TZ2unidentified phageQ859R8696020
the insoluble protein is solubilized in urea and purified by passing through a His-bind column, and the lytic activity is then restored by a refolding processXanthomonas phage Xop411A1BPG9682650

Cloned/COMMENTARY ORGANISM UNIPROT ACCESSION NO. LITERATURE
the mature peptide coding region is heterologously expressed in Escherichia coliApostichopus japonicus-709183
the gene encoding the Bacillus anthracis GH25 enzyme, BaGH25c, is expressed in Escherichia coliBacillus anthracis-708007
-Bos taurusQ06283697903
-Bufo andrewsi-664671
expression in Escherichia coliCanis lupus familiaris-171098
-Chlamys farreriQ075V3681964
ply3626 gene, expression in Escherichia coli JM109Clostridium phage phi3626-654265
expression in Escherichia coliColitis bacteriophage-171090
expression in Escherichia coliEnterobacteria phage phiKMV-664563
T4 lysozyme is cloned into the yeast expression vector pPIC9K under the control of the Pichia pastoris glyceraldehyde-3-phosphate dehydrogenase promoter and expressed at high level in Hansenula polymorpha strain A16, the enzyme is secretedEnterobacteria phage T4-718395
overexpression in Escherichia coliEquus caballus-710467
the gene coding for lysozyme in banana prawn (Fenneropenaeus merguiensis) is cloned, sequenced and expressed in pET-32a vector (Escherichia coli)Fenneropenaeus merguiensis-709875
a large polymannose (Man310GlcNAc2) chain-linked lysozyme is predominantly expressed in Saccharomyces cerevisiae accompanied by small amounts of a core-type oligomannose chain (Man14GlcNAc2)-linked lysozyme in the yeast medium where the extracellular pH is kept at 3.5 or above, while an oligomannose chain lysozyme is preferentially expressed in the yeast medium where the pH is less than 3Gallus gallus-679544
expression in human cell lines HeLa and MCF-7Gallus gallus-171038
expression in Saccharomyces cerevisiaeGallus gallus-698654
expression of recombinant protein in Saccharomyces cerevisiaeGallus gallus-171094
expression of wild-type and engineered enzyme in Saccharomyces cerevisiaeGallus gallus-171111
two serine-rich heptapeptides, Ser-Ser-Ser-Lys-Ser-Ser-Ser (S6K) and Ser-Ser-Ser-Ser-Ser-Ser-Ser (S7) are fused to the C-terminus of chicken lysozyme by genetic modification. The cDNAs of S6K-lysozyme and S7-lysozyme are inserted into the expression vector of Pichia pastoris and secreted in the yeast cultivation medium. The secretion amounts of S6K-lysozyme and S7-lysozyme are about 60% of that of wild-type lysozymeGallus gallus-664351
expression in Escherichia coliHelicoverpa armigeraQ19R28695906
-Helicoverpa zea-665818
2 different kinds of transgenic mice containing human lysozyme genomic DNA-based constructs with different signal peptide DNA are respectively established as system modelsHomo sapiens-681099
expression in goat at 67% of human breast milkHomo sapiens-699710
expression in Pichia pastorisHomo sapiens-677972
expression in Saccharomyces cerevisiaeHomo sapiens-171034, 171036
expression of the enzyme in transgenic cattle, Bos taurus, as secreted enzyme in milk using the pBC2-HLY-NEOR transgene vectorHomo sapiens-718276
recombinant expression of the mature peptide-coding region in Pichia pastoris strain GS115Homo sapiensQ86SG7718120
-Lactobacillus phage phigaY-680003
acmB gene, AcmB devoid of its N-terminal domain, expression in Escherichia coli M15(pREP4), sequencingLactococcus lactisQ8KKF9656731
expression in Pichia pastorisLarimichthys crocea-677863
-Musca domesticaB3GQR5699304
recombinant expression of wild-type and mutant MdL1 and MdL2 in Pichia pastorisMusca domestica-717509
a C-terminal hexahistidine tail Lys44 is overproduced in Escherichia coliOenococcus phage fOg44-680524
-Penaeus monodonQ8IT75700107
into the pQE-30 vector for expression in Escherichia coli cellsPseudomonas phage phiKZQ8SD18683684
Tapes japonica lysozyme (TjL) is recombinantly produced using Pichia pastoris YJT46Ruditapes philippinarum-708061
expression in Escherichia coliSalmo salar-679139
expression of 253 C-terminal residues in Escherichia coliStreptococcus pneumoniae-171051
the fragment is expressed in both BL21 (DE3) and B834 (DE3) Escherichia coli cellsStreptococcus pneumoniae-706988
amino acid Ser at the N-terminusStruthio camelus-697868
expression in Pichia pastorisStruthio camelus-680548
the His-tagged protein Lys411H is expressed in Escherichia coli mostly in inclusion bodiesXanthomonas phage Xop411A1BPG9682650

EXPRESSION ORGANISM UNIPROT ACCESSION NO. LITERATURE
No entries in this field

ENGINEERINGORGANISM UNIPROT ACCESSION NO.COMMENTARYLITERATURE
N44Q/N47Q/N49Q/N103QCanis lupus familiaris-mutant construcuted for study of charge heterogeneity caused by asparaginyl deamidation. Residues Asn 44, 47, 49, and 68 are the deamidation sites701125
N44Q/N47Q/N49Q/N68QCanis lupus familiaris-mutant construcuted for study of charge heterogeneity caused by asparaginyl deamidation. Residues Asn 44, 47, 49, and 68 are the deamidation sites701125
N44Q/N47Q/N49Q/N68Q/N103QCanis lupus familiaris-mutant construcuted for study of charge heterogeneity caused by asparaginyl deamidation. Residues Asn 44, 47, 49, and 68 are the deamidation sites. Decrease in lytic activity by a factor 20 compared with wild-type701125
N44Q/N47Q/N68Q/N103QCanis lupus familiaris-mutant construcuted for study of charge heterogeneity caused by asparaginyl deamidation. Residues Asn 44, 47, 49, and 68 are the deamidation sites701125
N44QN49Q/N68Q/N103QCanis lupus familiaris-mutant construcuted for study of charge heterogeneity caused by asparaginyl deamidation. Residues Asn 44, 47, 49, and 68 are the deamidation sites701125
A98LEnterobacteria phage T4-study on denatured state and its stabilization by high pressure. At pH 3.0, the magnitudes of the volume changes of denaturation for L99A, L99G/E108V, A98L, and V149G T4 lysozyme positively correlate with the total cavity volume696225
I3C/C54TEnterobacteria phage T4-reduction leads to destabilization171033
I3C/C54VEnterobacteria phage T4-reduction leads to destabilization171033
K60H/L13DEnterobacteria phage T4-destabilization171033
K83H/A112DEnterobacteria phage T4-destabilization171033
L99AEnterobacteria phage T4-study on denatured state and its stabilization by high pressure. At pH 3.0, the magnitudes of the volume changes of denaturation for L99A, L99G/E108V, A98L, and V149G T4 lysozyme positively correlate with the total cavity volume696225
N144EEnterobacteria phage T4-increased stability171033
Q123EEnterobacteria phage T4-increased stability171033
S90H/Q122DEnterobacteria phage T4-destabilization171033
T115EEnterobacteria phage T4-increased stability171033
K33AGallus gallus-140% of wild-type lytic activity, 116% of wild-type activity on glycol chitin698654
N103DGallus gallus-increased structural flexibility and surface functional properties171111
N106DGallus gallus-increased structural flexibility and surface functional properties171111
R114AGallus gallus-decrease in activity toward substrate glycol chitin to 80.5%. Reduction of binding free enrgies of E-F sites and the rate constant of transglycosylation for substrate GlcNAcbeta(1-4)GlcNAcbeta(1-4)GlcNAcbeta(1-4)GlcNAcbeta(1-4)GlcNAcbeta is about 50% of wild-type. Structural changes induced by the mutation are extended to aromatic side chains of F34 and W123696840
R114HGallus gallus-decrease in activity toward substrate glycol chitin to 79%. Reduction of binding free enrgies of E-F sites and the rate constant of transglycosylation for substrate GlcNAcbeta(1-4)GlcNAcbeta(1-4)GlcNAcbeta(1-4)GlcNAcbeta(1-4)GlcNAcbeta. Structural changes induced by the mutation are extended to aromatic side chains of F34 and W123696840
R114LGallus gallus-no decrease in activity toward substrate glycol chitin. Reduction of binding free enrgies of E-F sites and the rate constant of transglycosylation for substrate GlcNAcbeta(1-4)GlcNAcbeta(1-4)GlcNAcbeta(1-4)GlcNAcbeta(1-4)GlcNAcbeta696840
R21T/G49NGallus gallus-better emulsifying properties171094
A83K/Q86D/A92DHomo sapiens-decreased lytic activity at 1 mM CaCl2, but increased activity at 10 mM CaCl2171100
Q86DHomo sapiens-decreased lytic activity at 1 mM CaCl2171100
Q86D/A92DHomo sapiens-decreased lytic activity at 1 mM CaCl2, but increased activity at 10 mM CaCl2171100
R101D/R115HHomo sapiens-the charge engineered variant's two mutated amino acids exhibit stabilizing interactions with adjacent native residues, the mutant shows severalfold increased activity compared to the wild-type enzyme, the mutations cause no gross structural perturbations or loss of stability, but dramatically expand the negative electrostatic potential that, in the wild-type enzyme, is restricted to a small region near the catalytic residues. Reduction in the overall strength of the engineered enzyme's electrostatic potential field, the specific nature of this remodeled field underlies the variant’s reduced susceptibility to inhibition by anionic biopolymers, overview. The double mutant lyses bacteria effectively at alginate, mucin and DNA concentrations that inactivate wild-type enzyme. The mutations does not substantially impair the enzyme’s Vmax or Km, has no effect on its in vitro anti-pseudomonal activity, and does not reduce lytic function718273
_K1insAHomo sapiens-the pH-profile is almost the same as that of native enzyme682197
_K1insKHomo sapiens-the optimal pH-range is extended to higher pH-values in comparison to wild-type enzyme and mutant enzyme _K1insN. The mutant enzyme has significantly higher activity than native enzyme and _K1insN in higher ionic strength and in 150 mM NaCl. The mutant enzyme may be a useful antimicrobial agent682197
_K1insLHomo sapiens-the pH-profile is almost the same as that of native enzyme682197
_K1insNHomo sapiens-the pH-profile is almost the same as that of native enzyme682197
_K1insVHomo sapiens-the pH-profile is almost the same as that of native enzyme682197
D12ALactobacillus phage phigaY-cell-lytic activity is strongly reduced680003
D12A/E33ALactobacillus phage phigaY-no cell-lytic activity680003
D12GLactobacillus phage phigaY-cell-lytic activity isstrongly reduced680003
D198ALactobacillus phage phigaY-cell-lytic activity is slightly reduced680003
D36ALactobacillus phage phigaY-cell-lytic activity is similar to wild-type enzyme680003
D96ALactobacillus phage phigaY-cell-lytic activity is strongly reduced680003
E237ALactobacillus phage phigaY-cell-lytic activity is similar to wild-type enzyme680003
E238ALactobacillus phage phigaY-cell-lytic activity is similar to wild-type enzyme680003
E33ALactobacillus phage phigaY-cell-lytic activity isstrongly reduced680003
E88DLactobacillus phage phigaY-cell-lytic activity is similar to wild-type enzyme680003
E98ALactobacillus phage phigaY-no cell-lytic activity680003
G10SLactobacillus phage phigaY-cell-lytic activity is strongly reduced680003
G253ALactobacillus phage phigaY-cell-lytic activity is similar to wild-type enzyme680003
G267ALactobacillus phage phigaY-cell-lytic activity is similar to wild-type enzyme680003
G281ALactobacillus phage phigaY-cell-lytic activity is similar to wild-type enzyme680003
G292ALactobacillus phage phigaY-cell-lytic activity is similar to wild-type enzyme680003
H60RLactobacillus phage phigaY-cell-lytic activity is strongly reduced680003
K142ELactobacillus phage phigaY-cell-lytic activity is similar to wild-type enzyme680003
K142RLactobacillus phage phigaY-cell-lytic activity is similar to wild-type enzyme680003
K207ALactobacillus phage phigaY-cell-lytic activity is similar to wild-type enzyme680003
K211ALactobacillus phage phigaY-cell-lytic activity is similar to wild-type enzyme680003
K25TLactobacillus phage phigaY-cell-lytic activity is similar to wild-type enzyme680003
L132PLactobacillus phage phigaY-cell-lytic activity is strongly reduced680003
L264ALactobacillus phage phigaY-cell-lytic activity is slightly reduced680003
M1ILactobacillus phage phigaY-cell-lytic activity is reduced680003
N67KLactobacillus phage phigaY-cell-lytic activity is similar to wild-type enzyme680003
P212ALactobacillus phage phigaY-cell-lytic activity is similar to wild-type enzyme680003
P216ALactobacillus phage phigaY-cell-lytic activity is similar to wild-type enzyme680003
R109LLactobacillus phage phigaY-cell-lytic activity is similar to wild-type enzyme680003
R251ALactobacillus phage phigaY-cell-lytic activity is slightly reduced680003
V124MLactobacillus phage phigaY-cell-lytic activity is slightly reduced680003
V79FLactobacillus phage phigaY-cell-lytic activity is similar to wild-type enzyme680003
W284ALactobacillus phage phigaY-cell-lytic activity is strongly reduced680003
W284GLactobacillus phage phigaY-cell-lytic activity is strongly reduced680003
Y272ALactobacillus phage phigaY-cell-lytic activity is strongly reduced680003
N46D/S106V/T107AMusca domestica-site-directed mutagenesis of isozyme MdL2, the mutant pKas are increased compared to the wild-type pKas717509
D30ARuditapes philippinarum-mutant exhibits no lysozyme activity680812
E18ARuditapes philippinarum-mutant exhibits no lysozyme activity680812
C18S/C29SStruthio camelus-deletion of disulfide bond. No rearkable difference to wild-type in secondary structure or catalytic activity, but decrease in stability697868
C4S/C18S/C29S/C60SStruthio camelus-deletion of both disulfide bonds. No rearkable difference to wild-type in secondary structure or catalytic activity, but decrease in stability. Optimum temperature of catalytic activity is dow-shifted by about 20 degrees697868
C4S/C60SStruthio camelus-deletion of disulfide bond. No rearkable difference to wild-type in secondary structure or catalytic activity, but decrease in stability697868
E73AStruthio camelus-no hydrolysis of N,N',N'',N''',N''''-pentaacetylchitopentaose at 50°C for 48 h. Decrease in Tm-value is 3.2°C as compared to wild-type value680548
E73DStruthio camelus-detectable level of activity, but lytic activity against Micrococcus lysodeikticus is drastically reduced as compared to wild-type activity. Decrease in Tm-value is 6.1°C as compared to wild-type value680548
E73QStruthio camelus-no hydrolysis of N,N',N'',N''',N''''-pentaacetylchitopentaose at 50°C for 48 h. Decrease in Tm-value is 4.0°C as compared to wild-type value680548
N47Q/N49Q/N68Q/N103QCanis lupus familiaris-mutant construcuted for study of charge heterogeneity caused by asparaginyl deamidation. Residues Asn 44, 47, 49, and 68 are the deamidation sites701125
additional informationEnterobacteria phage K11-constructions of chimeric lysozymes are carried out by swapping the N-terminal and C-terminal domains between phage T7 and K11 lysozymes. This technique generates two chimeras, T7K11-lysozyme (N-terminal T7 domain and C-terminal K11 domain) and K11T7-lysozyme (N-terminal K11 domain and C-terminal T7 domain), which are both enzymatically active. The amidase activity of T7K11-lysozyme is comparable with the parental enzymes while K11T7-lysozyme exhibits an activity that is approximately 45% greater than the wild-type lysozymes. The chimeric constructs have optimum pH of 7.2-7.4 similar to the parental lysozymes but exhibit greater thermal stabilities. The chimeras inhibit transcription comparable with the parental lysozymes depending on the source of their N-terminals. Domain swapping technique localizes the N-terminal region as the domain responsible for the transcription inhibition specificity of the wild type T7 and K11 lysozymes680582
L99G/E108VEnterobacteria phage T4-study on denatured state and its stabilization by high pressure. At pH 3.0, the magnitudes of the volume changes of denaturation for L99A, L99G/E108V, A98L, and V149G T4 lysozyme positively correlate with the total cavity volume696225
additional informationEnterobacteria phage T4-L20 is a mutant with a molecular switch in a T4 lysozyme construct that promotes a large-scale (about 20 A) translocation of an alpha-helix but is unrelated to the function of the protein. The design is based in part on the use of a duplicated helical sequenc. When Arg63 is truncated to Ala (in mutant L20/R63A), the stability of the protein is reduced by 6.1°C relative to L20. In high salt buffer similar to that used for crystallization, the melting temperature of L20/R63A is increased by 2.2°C in the presence of either 200 mM methylguanidinium or 200 mM ethylguanidinium ion682730
V149GEnterobacteria phage T4-study on denatured state and its stabilization by high pressure. At pH 3.0, the magnitudes of the volume changes of denaturation for L99A, L99G/E108V, A98L, and V149G T4 lysozyme positively correlate with the total cavity volume696225
additional informationEnterobacteria phage T7-constructions of chimeric lysozymes are carried out by swapping the N-terminal and C-terminal domains between phage T7 and K11 lysozymes. This technique generates two chimeras, T7K11-lysozyme (N-terminal T7 domain and C-terminal K11 domain) and K11T7-lysozyme (N-terminal K11 domain and C-terminal T7 domain), which are both enzymatically active. The amidase activity of T7K11-lysozyme is comparable with the parental enzymes while K11T7-lysozyme exhibits an activity that is approximately 45% greater than the wild-type lysozymes. The chimeric constructs have optimum pH of 7.2-7.4 similar to the parental lysozymes but exhibit greater thermal stabilities. The chimeras inhibit transcription comparable with the parental lysozymes depending on the source of their N-terminals. Domain swapping technique localizes the N-terminal region as the domain responsible for the transcription inhibition specificity of the wild type T7 and K11 lysozymes680582
K33NGallus gallus-130% of wild-type lytic activity, 111% of wild-type activity on glycol chitin698654
additional informationGallus gallus-two serine-rich heptapeptides, Ser-Ser-Ser-Lys-Ser-Ser-Ser (S6K) and Ser-Ser-Ser-Ser-Ser-Ser-Ser (S7) are fused to the C-terminus of chicken lysozyme by genetic modification. The cDNAs of S6K-lysozyme and S7-lysozyme are inserted into the expression vector of Pichia pastoris and secreted in the yeast cultivation medium. The secretion amounts of S6K-lysozyme and S7-lysozyme are about 60% of that of wild-type lysozyme. The bactericidal activity against Escherichia coli of S6L-lysozyme and S7-lysozyme is greatly increased664351
additional informationGallus gallus-the lytic activities of the oligomannosyl lysozyme (a core-type oligomannose chain (Man14GlcNAc2)-linked lysozyme and) and the polymannosyl lysozymes (a large polymannose (Man310GlcNAc2) chain-linked lysozyme) are 70.4% and 5.1%, respectively, of the wild-type lysozyme when Micrococcus lysodeikticus cells are used as the substrate. The enzymatic activity of the oligomannosyl lysozyme is totally conserved for the glycolysis assay with a soluble substrate, glycol chitin, whereas that of the polymannosyl lysozyme is not. After heating the sample up to 95 °C at pH 7.0 where no visible protein coagulation is observed, thermostability of the enzymatic activity of the oligomannosyl lysozyme is drastically improved with more than 60% of residual lytic activity. Emulsifying properties of the protein also are highly improved by the oligomannosylation, in which the emulsifying activity is 3.2 times higher than that of the wild-type protein. Corresponding to the increase of the surface functionalities, the surface tension of the oligomannosyl protein exhibits a significantly lower value compared to that of the wild-type679544
additional informationGallus gallus-a oleyl group is covalently bound to free amino groups, N-terminal amino group and epsilon-amino groups of lysine residues, on lysozyme. No decrease in the activity of lysozyme derivatives occurs compared to native lysozyme, but the oleyl group, as a hydrophobic compound, facilitated the interaction of lysozyme with the bacterial membrane through hydrophobic interaction718309
A92DHomo sapiens-decreased lytic activity at 1 mM CaCl2171100
additional informationHomo sapiens-review about engineering of human lysozyme171110
additional informationHomo sapiens-a strategy to engineer an additional active site for human lysozyme: grafting the entire human lysozyme exon 2, which encodes the catalytically competent domain, into the gene at a position corresponding to an exposed loop region in the translated protein. Exon 2 grafting creates a novel lysozyme with twice the activity of the wild type enzyme, equal activity came from each of the two active sites. The thermal stability and pH-stability of wild-type and two-active site lysozyme is similar677972
additional informationHomo sapiens-production of secreted recombinant human lysozyme by use of overexpression vector pPIC3.5k, carrying the strong promoter AOX1 of aldehyde oxidase 1, the HSA signal peptide, the enterokinase recognition motif, and the lysozyme gene. Mature protein is identical with native human lysozyme. It exhibits in vitro bacteriolytic activity against the Gram-positive bacterium Micrococcus lysodeikticus and the Gram-negative bacterium Escherichia coli696869
M1KLactobacillus phage phigaY-cell-lytic activity is reduced680003
additional informationLactobacillus phage phigaY-deletion analysis demonstrates that the beta/alphagaY domain of N-terminal 216 residues is the core enzyme portion, although the cell-lytic ability is lower than that of LysgaY. These mutational experiments suggest that beta/alphagaY (in which two acidic residues of D12 and E98 likely act as catalytic residues) is responsible for cell-lytic activity, and SH3bgaY promotes beta/alphagaY possibly through cell-wall binding function680003
Y61HLactobacillus phage phigaY-cell-lytic activity is stronly reduced680003
additional informationLactococcus lactisQ8KKF9acmB deletion/insertion mutants with lower autolysis rate/extend656731
additional informationMusca domestica-introduction of six basic residues onMdL1 surface increases by 1 unit the pH optimum for the activity upon bacterial walls717509

Renatured/COMMENTARYORGANISM UNIPROT ACCESSION NO.LITERATURE
Cm value for guanidinium hydrochloride-induced unfolding is 3.1 M at pH 2.0, and 4.2 M at pH 6.0, respectivelyBos taurusQ06283697903
-Canis lupus familiaris-171098, 678277
on stretching from its N and C termini using single-molecule atomic force microscopy, T4 lysozyme unfolds by multiple distinct unfolding pathways: the majority of T4 lysozymes unfold in an all-or-none fashion by overcoming a dominant unfolding kinetic barrier; and a small fraction of T4 lysozymes unfold in three-state fashion involving unfolding intermediate states. Results give direct evidence for the kinetic partitioning of the mechanical unfolding pathways of T4 lysozyme, and the complex unfolding behaviors reflect the stochastic nature of kinetic barrier rupture in mechanical unfolding processesEnterobacteria phage T4-700964
reversible thermal denaturation conditions: acid pH, 0.2 M NaCl, 0.10 mM dithiothreitol, 0.01 mM T4 lysozymeEnterobacteria phage T4-171070
study on four mutants having different cavity volumes at low and neutral pH upto a pressure of 400 MPa. The pressure-denatured state at neutral pH is even more compact than at low pH, and the preferential filling of large cavities may be responsible for the compactness. Pressure denaturation is characteristically distinct from thermal or chemical denaturationEnterobacteria phage T4-696225
-Gallus gallus-171089
catalytic properties during renaturationGallus gallus-171106
characterization of the refolded hen lysozyme variant (4CAHEL) lacking two outside disulfide bonds (C6-C127 and C30-C115). 4CAHEL is a folding intermediated formed in the early stage of the refolding process of the reduced lysozymeGallus gallus-664368
crystallographic studies of denaturation and renaturationGallus gallus-171062, 171063
dithiothreitol decreases content of alpha-helices with a corresponding increase in random coil, while 2,2,2-trifluoroethanol has a negligible effect on secondary structureGallus gallus-696414
measurement of lysozyme solubility in aqueous solutions as a function of NaCl, KCl, and NH4Cl concentrations at 25°C and pH 4.5. The dependence of solubility on salt type and concentration strongly correlates with the corresponding dependence of the preferential interaction coefficient. The solubility dependence on salt concentration is substantially affected by the corresponding change of protein chemical potential in the crystalline phase. Simple model for the crystalline phase based on salt partitioning between solution and the hydrated protein crystalGallus gallus-698462
measurement of refolding after pressure unfolding. Pressure acts against aggregation and therefore no irreversible aggregation takes place during the pressure treatment. After the release of the pressure, folding intermediate structures are found which are formed during the decompression of the lysozyme. The intermediates are only formed if the protein is unfolded, subdenaturing pressure can not populate this intermediatesGallus gallus-678407
neutral cyclodextrins are better refolding agents than the charged sugars. The presence of anionic substitutents like carboxy and phosphate groups promote aggregate formation and completely abolish the refolding ability of the sugars. Cyclodextrins with cationic functional groups do not show any significant effects on lysozyme refolding. The presence of both anionic and cationic substituents on the same cyclodextrin molecule partially restores its renaturation abilityGallus gallus-678484
no noticeable enhancement in enzyme activity and stability in the presence of supercritical CO2 pretreatment for lysozyme samples denatured in 8 M urea at 50°C and pH 6.2. Supercritical CO2 pretreated lysozyme samples in 0.067 M phosphate buffer containing dithiothreitol at 0.1 M, pH 6.2, 25°C or 0.01 M dithiothreitol, pH 6.2, 50 °C at 2500 psi and 50°C have better residual activity relative to samples that are not pretreated. In addition, when denaturing at 65°C and pH 9.0, the pretreatment in supercritical CO2 at 2500 psi and 50°C results in the best stability of lysozymeGallus gallus-699054
oxidative refolding carried out in presence of protein disulfide isomerase results in an increased refolding rate and a recovered activity exceeding 100%. Refolding is achieved through the formation of protein disulfide isomerase-lysozyme intermediates and the excess activity is derived from the nascent lysozyme released from these complexesGallus gallus-699048
production of a three-disulfid derivativeGallus gallus-171107
stabilizing effect of cross-linked enzymeGallus gallus-171103
study on guanidinium chloride-induced equilibrium unfolding of monomer and dimer at pH 2.0. Unfolding curves at 222 and 289 nm in lysozyme dimer lack coincidence, while lysozyme monomer shows a single cooperative transition. Kinetic parameters are calculated on basis of a two-state mechanism for monomer and a three-state mechanism for dimer. Zero length cross-linking can stabilize the intermediateGallus gallus-696408
the refolding rate increases with an increase in concentration of protein disulfide isomerase. About 100% activity is recovered after 10 min initiation of the reaction at 0.062 mM protein disulfide isomerase, whereas several hours are needed for 100% activity recovery in absence of protein disulfide isomeraseGallus gallus-680954
thermodynamic analysis of unfolding in presence of GdnHClGallus gallus-717672
characterization of oligomers obtained after 5 days incubation at pH 3.0 and 60°C. Oligomers are misfolded species when compared to monomeric lysozyme, with a prevalence of random structure but with significant elements of the beta-sheet structure that is characteristic of the mature fibrils. The oligomeric lysozyme aggregates are more susceptible to proteolysis with pepsin than both the monomeric protein and the mature fibrilsHomo sapiens-699576
unfolding and potential refolding analysis due to cold adaptation and heat treatment, differential scanning calorimetry. Recombinant SalG has a melting temperature of 36.8°C under thermal denaturation conditions and regains activity after returning to permissive (low) temperature. Refolding is dramatically reduced in solutions with high SalG concentrations, coupled with significant protein precipitation. Rapid and irreversible inactivation takes place during heating at high enzyme concentrationSalmo salarA6PZ97717510
the cell wall binding module is intrinsically unstable, and the ultimate folding and stabilization of the active, monomeric form of the enzyme relies on choline binding. Complex formation proceeds in a rather slow way, and all sites behave as equivalentStreptococcus pneumoniae-698818
when the thermal denaturation curves are analyzed in the absence of guanidine hydrochloride, the reversibility calculated is 76% for the wild-type enzyme, 80% for E73D, 80% for E73Q and 79% for E73A. In the presence of 0.5 M guanidine hydrochloride, the reversibility of the thermal unfolding for the wild type and mutant proteins is more than 95%Struthio camelus-680548

APPLICATIONORGANISM UNIPROT ACCESSION NO.COMMENTARYLITERATURE
food industryBacillus sp.-the LD50 value of lysozyme is 4530 mg/kg body weight. 90 days of marine low-temperature lysozyme treatment at three doses shows no significant difference on blood biochemistry and organ index in drug treatment groups compared to saline treatment group. Marine low-temperature lysozyme can be safely used at the dose of experiment applied in food industry and further clinical studies679957
medicineBacillus sp.-the marine lysozyme is a potent antitumor molecule, which may inhibit tumor growth and inhibit angiogenesis. This lysozyme may have a therapeutic value in antitumor drug development677778
nutritionClostridium phage phi3626-Ply3626, which is highly specific towards Clostridium perfringens strains, might be useful for novel biocontrol measures in food, feed, and complex microbial communities, application as a novel biopreservative in food items such as raw chicken or turkey654265
nutritionEnterobacteria phage phiKMV-because of the capacity to withstand prolonged heat treatment the enzyme may be used in food conservation (hurdle technologies) against Gram-negative bacteria664563
analysisGallus gallus-cross-linking method for lysozyme and catalytic activity assay. Catalytic activity of lysozyme dimer is the same as monomer696408
analysisGallus gallus-kinetics of tertiary conformation of lysozyme adsorbed on 90 nm silica nanoparticles. A rapid initial unfolding, followed by a much slower refolding and subsequent unfolding is observed, with the extent of unfolding being higher at lower surface concentration, higher ionic strengths, higher 2,2,2-trifluoroethanol and dithiothreitol concentrations and at pH 9. alpha-Helix content is lower for adsorbed lysozyme compared to bulk with a corresponding increase in beta-sheet and random coil696414
food industryGallus gallus-dry-heated hen egg white lysozyme simultaneously exhibits enhanced foaming properties and aggregation capacity. It may self-associate at the air/water interface, stabilizing air bubbles698409
industryGallus gallus-immobilization of lysozyme to the surface of stainless steel as a new strategy to protect the surface against the growth of biofilms663529
medicineGallus gallus-influence of carboxylic acid and ester groups at the end of poly lactic acid/poly (DL-lactide-co-glycolide) based polymer on the rate of release and biological activity of lysozyme as a model protein from in situ gel forming controlled release formulations680255
medicineGallus gallus-by inhibiting Clostridium perfringens type A and its alpha-toxin production, hen egg white lysozyme shows potential for use in the treatment and prevention of necrotic enteritis and other Clostridium perfringens type A related animal diseases681709
synthesisGallus gallus-the extracellular pH-sensitive glycosylation system can be used to obtain bioactive and surface functional neoglycoproteins679544
analysisHomo sapiens-establishment of a precise fluorimetric assay for determination and characterisation of lysozyme activity immobilised in the initial in situ formed pellicle. For in situ pellicle formation, bovine enamel slabs were fixed on maxillary splints and carried by six subjects for different times on buccal and palatal sites. The mean immobilised activity over all samples amounted to 68.67 U/cm2. The enzyme activity exposed at the pellicles' surfaces increases in a time-dependant manner and shows a Michaelis-Menten kinetic. Chlorhexidine and black tea reduce lysozyme activity of the in situ pellicle significantly697428
medicineHomo sapiens-establishment of a precise fluorimetric assay for determination and characterisation of lysozyme activity immobilised in the initial in situ formed pellicle. For in situ pellicle formation, bovine enamel slabs were fixed on maxillary splints and carried by six subjects for different times on buccal and palatal sites. The mean immobilised activity over all samples amounted to 68.67 U/cm2. The enzyme activity exposed at the pellicles' surfaces increases in a time-dependant manner and shows a Michaelis-Menten kinetic. Chlorhexidine and black tea reduce lysozyme activity of the in situ pellicle significantly697428
nutritionHomo sapiens-feeding of pigs with a diet of solid food and goat's milk of transgenic animals expressing human lysozyme results in fewer total coliforms and Escherichia coli in the ileum and in a greater duodenal width after infection with Escherichia coli. Control pigs receiving transgenic milk have fewer intraepithelial lymphocytes per micron of villi weight than animlas receiving control milk699710
synthesisHomo sapiens-production of secreted recombinant human lysozyme by use of overexpression vector pPIC3.5k, carrying the strong promoter AOX1 of aldehyde oxidase 1, the HSA signal peptide, the enterokinase recognition motif, and the lysozyme gene. Mature protein is identical with native human lysozyme. It exhibits in vitro bacteriolytic activity against the Gram-positive bacterium Micrococcus lysodeikticus and the Gram-negative bacterium Escherichia coli696869
medicinePseudomonas phage phiKZQ8SD18the structure of gp144 might be useful for the development of new antibacterial reagents for preventing and treating Pseudomonas aeruginosa infections683684
agricultureXanthomonas phage Xop411A1BPG9Lys411H is the first lysozyme active against both Xanthomonas and Stenotrophomonas maltophilia. This suggests that Lys411 can be a candidate to be developed into a therapeutic agent for treating Stenotrophomonas maltophilia infections, in addition to the potential use in control of the plant diseases caused by Xanthomonas682650
medicineGallus gallus-Hen egg white lysozyme amyloid fibrils cause extensive aggregation of human erythrocytes and lipid vesicles without any significant lysis. The membrane activity of lysozyme fibrils suggests that the interaction of lysozyme fibrils with cellular membranes could be a contributing factor under conditions of human lysozyme amyloidosis700151
additional informationGallus gallus-adsorption studies are conducted to investigate the effects of shaking rate, temperature, and initial lysozyme concentration on the uptake rate of lysozyme by the NaY zeolite (immobilization support)682603

DISEASETITLE OF PUBLICATIONLINK TO PUBMED
AbscessA biologic basis for altered host defenses in surgically infected abscesses. PubMed
AbscessConstituent analysis may permit improved diagnosis of intra-abdominal abscess. PubMed
AbscessDetection of intraabdominal abscess by serum lysozyme estimation. PubMed
AbscessIncreased serum lysozyme in the presence of abscesses. PubMed
Abscess[Use of immobilized lysozyme in the treatment of suppurative wounds of the soft tissues] PubMed
AcidosisCoordinately increased lysozymuria and lysosomal enzymuria induced by maleic acid. PubMed
Acidosis, Renal TubularCoordinately increased lysozymuria and lysosomal enzymuria induced by maleic acid. PubMed
Acne VulgarisA method for the assay of inflammatory mediators in follicular casts. PubMed
Acquired Immunodeficiency SyndromeConstituent analysis may permit improved diagnosis of intra-abdominal abscess. PubMed
Acquired Immunodeficiency SyndromeEffect of organic acids in the prevention of aggregation on rapid refolding of proteins. PubMed
Acquired Immunodeficiency SyndromeElevated beta 2-microglobulin and lysozyme levels in patients with acquired immune deficiency syndrome. PubMed
Acquired Immunodeficiency SyndromeFiltration and local synthesis of lacrimal proteins in acquired immunodeficiency syndrome. PubMed
Acquired Immunodeficiency SyndromeLeukocyte subset analysis and related immunological findings in acquired immunodeficiency disease syndrome (AIDS) and malignancies. PubMed
Acquired Immunodeficiency SyndromeLysozyme association with nucleic acids. PubMed
Acquired Immunodeficiency SyndromeRefolding kinetics of denatured-reduced lysozyme in the presence of folding aids. PubMed
Acquired Immunodeficiency Syndrome[Serum and lacrimal proteins in acquired immunodeficiency syndrome] PubMed
Acrodermatitis[Lysozyme concentrations in the intestinal mucosa in malabsorption syndromes and chronic inflammatory intestinal diseases] PubMed
AcrospiromaImmunohistochemical study of lysozyme in various benign sweat apparatus tumors. PubMed
Acute Kidney InjuryEarly nephrotoxicity at high plasma concentrations of lysozyme in the rat. PubMed
Acute Kidney InjurySpecimen collection time for enzyme analysis in urine. PubMed
Acute Kidney InjuryUrine and serum lysozyme alterations in a case of acute renal failure. PubMed
Acute Kidney Injury[Functional recovery phase of acute renal insufficiency. Behavior and significance of urinary excretion of alpha-glucosidase, gamma-glutamyltransferase, lysozyme and beta 2 microglobulin] PubMed
AdenocarcinomaA new view of the so-called adenoma malignum of the uterine cervix. PubMed
AdenocarcinomaDiagnostic applications of an immunoperoxidase method in hematopathology. PubMed
AdenocarcinomaDistribution of lysozyme, alpha 1-Antichymotrypsin and alpha 1-Antitrypsin in adenocarcinomas of the stomach and large intestine. An immunohistochemical study. PubMed
AdenocarcinomaEndocrine cells and lysozyme immunoreactivity in the gallbladder. PubMed
AdenocarcinomaFrog lysozyme. IV. Isozyme of lysozyme and the Lucké renal adenocarcinoma. PubMed
AdenocarcinomaGastric carcinoma: histopathology, immunocytochemistry and variations of nucleolar organizer regions (AgNORs). PubMed
AdenocarcinomaIdentification of neoplastic Paneth cells in an adenocarcinoma of the stomach using lysozyme as a marker, and electron microscopy. PubMed
AdenocarcinomaIn vitro down regulation of ICAM-1 and E-cadherin and in vivo reduction of lung metastases of TS/A adenocarcinoma by a lysozyme derivative. PubMed
AdenocarcinomaIsolation of tumor-secreted products from human carcinoma cells maintained in a defined protein-free medium. PubMed
AdenocarcinomaLysozyme and secretory component in endocervical and endometrial adenocarcinoma. PubMed
AdenocarcinomaLysozyme in neoplastic Paneth cells of a jejunal adenocarcinoma. PubMed
AdenocarcinomaLysozyme: a major secretory product of a human colon carcinoma cell line. PubMed
AdenocarcinomaMixed mucinous-type and non-mucinous-type adenocarcinoma of the lung: immunohistochemical examination and K- ras gene mutation. PubMed
AdenocarcinomaPaneth cell-like change of the prostate gland. A histological, immunohistochemical, and electron microscopic study. PubMed
AdenocarcinomaPhenotypic characteristics of mouse lung adenoma induced by 4-(methylnitrosamino)-1-(3-pyridyl)-1-butanone. PubMed
AdenocarcinomaThe cellular response to human colonic neoplasms: macrophage numbers. PubMed
AdenocarcinomaThe immunohistochemical profile of the adenocarcinoma of upper gastric pole. PubMed
AdenocarcinomaTowards local electromechanical probing of cellular and biomolecular systems in a liquid environment. PubMed
AdenocarcinomaTubular adenoma of the human stomach. An immunohistochemical analysis of gut hormones, serotonin, carcinoembryonic antigen, secretory component, and lysozyme. PubMed
AdenocarcinomaUp-regulation of lysozyme production in colonic adenomas and adenocarcinomas. PubMed
Adenocarcinoma[A study on the mechanism of invasion of colorectal mucinous adenocarcinoma] PubMed
Adenocarcinoma[Malignant mesothelioma of the pleura. Analysis of its immunohistochemical aspects] PubMed
Adenocarcinoma, Mucinous[A study on the mechanism of invasion of colorectal mucinous adenocarcinoma] PubMed
Adenocarcinoma, ScirrhousScirrhous argyrophil cell carcinoma of the stomach with multiple production of polypeptide hormones, amine, CEA, lysozyme, and HCG. PubMed
AdenofibromaAltered monocyte function in patients with benign breast disease. PubMed
AdenomaCell lineage markers in premalignant and malignant colonic mucosa. PubMed
AdenomaColorectal adenomas produce lysozyme. PubMed
AdenomaDo stem cells participate in cell turnover in duodenal adenomas? A preliminary study on Paneth cells. PubMed
AdenomaExpression of calnexin reflects paneth cell differentiation and function. PubMed
AdenomaImmunohistochemical study on sebaceous adenoma and sebaceous carcinoma arising in parotid gland. PubMed
AdenomaIntestinal adenomas of Min-mice lack enterochromaffin cells, and have increased lysozyme production in non-Paneth cells. PubMed
AdenomaLactoferrin, lysozyme, and beta 2-microglobulin levels in cerebrospinal fluid: differential indices of CNS inflammation. PubMed
AdenomaLysozyme and mucins in gastric adenomas. PubMed
AdenomaLysozyme-rich muciphages surrounding colorectal adenomas. PubMed
AdenomaMyoepitheliomas and myoepithelial adenomas of salivary gland origin. Immunohistochemical evaluation of filament proteins, S-100 alpha and beta, glial fibrillary acidic proteins, neuron-specific enolase, and lactoferrin. PubMed
AdenomaPapillary adenoma of the stomach. Pathologic and immunohistochemical study. PubMed
AdenomaPhenotypic characteristics of mouse lung adenoma induced by 4-(methylnitrosamino)-1-(3-pyridyl)-1-butanone. PubMed
AdenomaProliferative characteristics of differentiated cells in familial adenomatous polyposis-associated duodenal adenomas. PubMed
AdenomaThe cellular response to human colonic neoplasms: macrophage numbers. PubMed
AdenomaThe Role of Cell Proliferation and Crypt Fission in Adenoma Aggressiveness: a Comparison of Ileoanal Pouch and Rectal Adenomas in FAP. PubMed
AdenomaTubular adenoma of the human stomach. An immunohistochemical analysis of gut hormones, serotonin, carcinoembryonic antigen, secretory component, and lysozyme. PubMed
AdenomaUp-regulation of lysozyme production in colonic adenomas and adenocarcinomas. PubMed
Adenoma, Liver CellKupffer cells in hepatocellular adenomas. PubMed
Adenoma, PleomorphicImmunofluorescence study of secretory epithelial markers in pleomorphic adenomas. PubMed
Adenoma, PleomorphicImmunohistochemical characterization of functional markers in human minor salivary gland tumors. PubMed
Adenoma, PleomorphicImmunohistochemical demonstration of lysozyme and lactoferrin in salivary pleomorphic adenomas. PubMed
Adenoma, PleomorphicImmunohistochemical investigation of lysozyme, lactoferrin, alpha 1-antitrypsin, alpha 1-antichymotrypsin and ferritin in parotid gland tumors. PubMed
Adenoma, PleomorphicImmunohistochemical localization of alpha 1-antitrypsin and alpha 1-antichymotrypsin in salivary pleomorphic adenomas. PubMed
Adenoma, PleomorphicImmunohistochemical localization of carcinoembryonic antigen in carcinoma in pleomorphic adenoma of salivary gland: use in the diagnosis of benign and malignant lesions. PubMed
Adenoma, PleomorphicImmunohistochemical study of four histologic types of parotid gland pleomorphic adenoma. PubMed
Adenoma, PleomorphicVarious expressions of modified myoepithelial cells in salivary pleomorphic adenoma. Immunohistochemical studies. PubMed
Adenoma, Pleomorphic[Biochemical findings in proteincomposition of secretions of human malignant parotid tumours, chronic parotitis and sialadenoses (author's transl)] PubMed
Adenoma, VillousColorectal adenomas produce lysozyme. PubMed
Aggressive PeriodontitisLysozyme and lactoferrin quantitation in the crevicular fluid. PubMed
Aggressive PeriodontitisPeroxidases, lactoferrin and lysozyme in peripheral blood neutrophils, gingival crevicular fluid and whole saliva of patients with localized juvenile periodontitis. PubMed
Aggressive Periodontitis[Microbiological data and mixed saliva lysozyme activity in periodontosis in workers from different occupations] PubMed
AgranulocytosisMuramidase activity in granulocytopenia. PubMed
AgranulocytosisStudies of lysozyme activity in serum, urine and blood smears from patients with haematological diseases (author's transl)] PubMed
Agranulocytosis[Muramidase activity in granulocytopenia] PubMed
AIDS-Related ComplexElevated beta 2-microglobulin and lysozyme levels in patients with acquired immune deficiency syndrome. PubMed
AlbuminuriaEarly indicators of renal damage in workers exposed to organic solvents. PubMed
AlbuminuriaEffects of glucocorticoid administration on urinary albumin excretion by the normal kidney. PubMed
AlbuminuriaFurther evidence for tubular dysfunction in insulin dependent diabetes. PubMed
Alzheimer DiseaseAutoimmune responses to amyloid structures of Abeta(25-35) peptide and human lysozyme in the serum of patients with progressive Alzheimer's disease. PubMed
Alzheimer DiseaseMacrophage markers in diagnostic neuropathology. PubMed
Alzheimer DiseasePopulation of nonnative states of lysozyme variants drives amyloid fibril formation. PubMed
Alzheimer DiseaseUniversal isolation of cross-linked peptides: application to neurofibrillary tangles. PubMed
AmyloidosisA camelid antibody fragment inhibits the formation of amyloid fibrils by human lysozyme. PubMed
AmyloidosisA family with gastrointestinal amyloidosis associated with variant lysozyme. PubMed
AmyloidosisA highly amyloidogenic region of hen lysozyme. PubMed
AmyloidosisA new human hereditary amyloidosis: the result of a stop-codon mutation in the apolipoprotein AII gene. PubMed
AmyloidosisA new lysozyme tyr54asn mutation causing amyloidosis in a family of Swedish ancestry with gastrointestinal symptoms. PubMed
AmyloidosisA novel lysozyme mutation Phe57Ile associated with hereditary renal amyloidosis. PubMed
AmyloidosisALys amyloidosis caused by compound heterozygosity in exon 2 (Thr70Asn) and exon 4 (Trp112Arg) of the lysozyme gene. PubMed
AmyloidosisAmyloidosis of the gastrointestinal tract: a 13-year single center referral experience. PubMed
AmyloidosisAn Insight into the pathway of the amyloid fibril formation of hen egg white lysozyme obtained from a small-angle X-ray and neutron scattering study. PubMed
AmyloidosisATP-induced noncooperative thermal unfolding of hen lysozyme. PubMed
AmyloidosisCharacterization of the structure and dynamics of amyloidogenic variants of human lysozyme by NMR spectroscopy. PubMed
AmyloidosisDisease-related amyloidogenic variants of human lysozyme trigger the unfolded protein response and disturb eye development in Drosophila melanogaster. PubMed
AmyloidosisEffects of oligomeric lysozyme on structural state of model membranes. PubMed
AmyloidosisEmergency liver transplantation for hereditary lysozyme amyloidosis. PubMed
AmyloidosisEngineering a camelid antibody fragment that binds to the active site of human lysozyme and inhibits its conversion into amyloid fibrils. PubMed
AmyloidosisFormation of amyloid aggregates from human lysozyme and its disease-associated variants using hydrostatic pressure. PubMed
AmyloidosisHeat-induced conversion of beta(2)-microglobulin and hen egg-white lysozyme into amyloid fibrils. PubMed
AmyloidosisHereditary lysozyme amyloidosis - phenotypic heterogeneity and the role of solid organ transplantation. PubMed
AmyloidosisHereditary lysozyme amyloidosis: spontaneous hepatic rupture (15 years apart) in mother and daughter. role of emergency liver transplantation. PubMed
AmyloidosisHereditary renal amyloidosis associated with variant lysozyme in a large English family. PubMed
AmyloidosisHereditary renal amyloidosis caused by a new variant lysozyme W64R in a French family. PubMed
AmyloidosisHuman lysozyme gene mutations cause hereditary systemic amyloidosis. PubMed
AmyloidosisIdentification of the core structure of lysozyme amyloid fibrils by proteolysis. PubMed
AmyloidosisInsights into the Conformational Changes of Several Human Lysozyme Variants Associated with Hereditary Systemic Amyloidosis. PubMed
AmyloidosisLeukocyte Chemotactic Factor 2 (LECT2)-Associated Renal Amyloidosis: A Case Series. PubMed
AmyloidosisLiver biopsy discloses a new apolipoprotein A-I hereditary amyloidosis in several unrelated Italian families. PubMed
AmyloidosisLocal cooperativity in an amyloidogenic state of human lysozyme observed at atomic resolution. PubMed
AmyloidosisLysozyme A model protein for amyloid research. PubMed
AmyloidosisLysozyme amyloid oligomers and fibrils induce cellular death via different apoptotic/necrotic pathways. PubMed
AmyloidosisLysozyme amyloidosis: report of 4 cases and a review of the literature. PubMed
AmyloidosisMedullary amyloidosis associated with apolipoprotein A-IV deposition. PubMed
AmyloidosisMetabolism of amyloid proteins. PubMed
AmyloidosisMethods and models in neurodegenerative and systemic protein aggregation diseases. PubMed
AmyloidosisMisdiagnosis of hereditary amyloidosis as AL (primary) amyloidosis. PubMed
AmyloidosisNative-State Stability Determines the Extent of Degradation Relative to Secretion of Protein Variants from Pichia pastoris. PubMed
AmyloidosisNormal and aberrant biological self-assembly: insights from studies of human lysozyme and its amyloidogenic variants. PubMed
AmyloidosisOstertag revisited: the inherited systemic amyloidoses without neuropathy. PubMed
AmyloidosisPattern similarity study of functional sites in protein sequences: lysozymes and cystatins. PubMed
AmyloidosisPeripheral genotype-phenotype correlations in Asian Indians with type 2 diabetes mellitus. PubMed
AmyloidosisPopulation of nonnative states of lysozyme variants drives amyloid fibril formation. PubMed
AmyloidosisPressure-jump NMR study of dissociation and association of amyloid protofibrils. PubMed
AmyloidosisRationalising lysozyme amyloidosis: insights from the structure and solution dynamics of T70N lysozyme. PubMed
AmyloidosisSeeking confidence in the diagnosis of systemic AL (Ig light-chain) amyloidosis: patients can have both monoclonal gammopathies and hereditary amyloid proteins. PubMed
AmyloidosisSimulations of human lysozyme: probing the conformations triggering amyloidosis. PubMed
AmyloidosisSmall molecule inhibitors of lysozyme amyloid aggregation. PubMed
AmyloidosisSpatial extent of charge repulsion regulates assembly pathways for lysozyme amyloid fibrils. PubMed
AmyloidosisStructural analysis of human lysozyme using molecular dynamics simulations. PubMed
AmyloidosisStructural diversity of ex vivo amyloid fibrils studied by cryo-electron microscopy. PubMed
AmyloidosisSuppression of lysozyme aggregation at alkaline pH by tri-N-acetylchitotriose. PubMed
AmyloidosisThe non-core regions of human lysozyme amyloid fibrils influence cytotoxicity. PubMed
AmyloidosisUnderdiagnosed amyloidosis: amyloidosis of lysozyme variant. PubMed
Amyloidosis, FamilialA non-natural variant of human lysozyme (I59T) mimics the in vitro behaviour of the I56T variant that is responsible for a form of familial amyloidosis. PubMed
Amyloidosis, FamilialAmyloidosis. PubMed
Amyloidosis, FamilialHereditary renal amyloidosis caused by a new variant lysozyme W64R in a French family. PubMed
Amyloidosis, FamilialLysozyme amyloidosis: report of 4 cases and a review of the literature. PubMed
AnaphylaxisActivation and consumption of Hageman factor in the anaphylactic shock of the rat. PubMed
AnaphylaxisLack of correlation between mast cell response and active anaphylaxis in mice. PubMed
AnaphylaxisPreventive effects of Impatiens balsamina on the hen egg-white lysozyme (HEL)-induced decrease in blood flow. PubMed
AnaphylaxisThrombocytopenia provoked by carrageenan in rabbits and the inhibitory effect of lysozyme. PubMed
Anaphylaxis[Data on a study of the nature of secondary immunodeficient states. I. An immunophysiological analysis of the mechanisms of allergic reaction suppression in experimental lesion of the structures of the dorsal hippocampus] PubMed
Anaphylaxis[Food additive hypersenisivity--near myth] PubMed
AnemiaChronic myelomonocytic leukemia according to FAB classification: analysis of 35 cases. PubMed
AnemiaIncreased in vivo activation of neutrophils and complement in sickle cell disease. PubMed
AnemiaPeripheral genotype-phenotype correlations in Asian Indians with type 2 diabetes mellitus. PubMed
AnemiaSickle cell anemia; sickle-cell-accelerating factor and its relationship to lysozyme. PubMed
Anemia[Acute myelomonocytic leukemia (M4) with CD19 antigen expression, eosinophilia and basophilia in bone marrow] PubMed
Anemia[So-called Ph1-negative chronic myelogenous leukemia with a mosaic pattern of trisomy 8 and normal karyotypes--report of 2 cases] PubMed
Anemia, Hemolytic, AutoimmunePartial tolerance of autoreactive B and T cells to erythrocyte-specificself-antigens in mice. PubMed
Anemia, MegaloblasticSignificance of changes in serum muramidase activity in megaloblastic anemia. PubMed
Anemia, PerniciousSerum lysozyme in inflammatory gastric and enteric diseases and in functional dyspepsia. PubMed
Anemia, Refractory[Serum muramidase assay in patients with refractory anaemia (author's transl)] PubMed
Anemia, Refractory, with Excess of BlastsUnsuspected gastric granulocytic sarcoma in a patient with myelodysplastic syndrome. PubMed
Anemia, Sickle CellIncreased in vivo activation of neutrophils and complement in sickle cell disease. PubMed
Anemia, Sickle CellSickle cell anemia; sickle-cell-accelerating factor and its relationship to lysozyme. PubMed
AnencephalyAmniotic fluid lysozyme content in normal and abnormal pregnancy. PubMed
AneurysmKawasaki Disease. PubMed
AngioedemaRecurrent angioedema due to lysozyme allergy. PubMed
AngiofibromaAlpha 1-antitrypsin and lysozyme in fibrous papules and angiofibromas. PubMed
Anthrax[The nonspecific resistance indices of different species of laboratory animals immunized with STI anthrax vaccine] PubMed
Anuria[Hemofiltration of lysozyme in dialysis patients] PubMed
ArteritisGiant-cell arteritis. Histological, immunohistochemical and electronmicroscopic studies. PubMed
ArthritisAllergic arthritis induced by cationic proteins: role of molecular weight. PubMed
ArthritisAnergy of antigen-specific T lymphocytes is a potent mechanism of intravenously induced tolerance. PubMed
ArthritisBacterial cell wall composition, lysozyme resistance, and the induction of chronic arthritis in rats. PubMed
ArthritisCharacterisation of Eubacterium cell wall: peptidoglycan structure determines arthritogenicity. PubMed
ArthritisClinical correlates and substrate specificities of antibodies exhibiting neutrophil nuclear rea