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Information on EC 3.2.1.17 - lysozyme and Organism(s) Mus musculus

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EC Tree
     3 Hydrolases
         3.2 Glycosylases
             3.2.1 Glycosidases, i.e. enzymes that hydrolyse O- and S-glycosyl compounds
                3.2.1.17 lysozyme
IUBMB Comments
cf. also EC 3.2.1.14 chitinase.
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This record set is specific for:
Mus musculus
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Word Map
The taxonomic range for the selected organisms is: Mus musculus
The enzyme appears in selected viruses and cellular organisms
Synonyms
lysozyme, endolysin, autolysin, t4 lysozyme, transglycosylase, muramidase, peptidoglycan hydrolase, lysozyme a, mutanolysin, lysozyme c, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
1,4-beta-N-acetylmuramidase
-
-
-
-
1,4-beta-N-acetylmuramidase A/C
-
-
-
-
1,4-beta-N-acetylmuramidase M1
-
-
-
-
1,4-beta-N-acetylmuramoylhydrolase
-
-
-
-
1,4-N-acetylmuramidase
-
-
-
-
Autolysin
-
-
-
-
CP-1 lysin
-
-
-
-
CP-7 lysin
-
-
-
-
CP-9 lysin
-
-
-
-
CPL
-
-
-
-
endolysin
-
-
-
-
globulin G
-
-
-
-
globulin G1
-
-
-
-
Goose-type lysozyme
-
-
-
-
L-7001
-
-
-
-
Late protein gp15
-
-
-
-
Lysis protein
-
-
-
-
Lysosyme
-
-
-
-
Lysozyme
-
-
-
-
lysozyme g
-
-
-
-
mucopeptide glucohydrolase
-
-
-
-
mucopeptide N-acetylmuramoylhydrolase
-
-
-
-
muramidase
-
-
-
-
MV1 lysin
-
-
-
-
N,O-diacetylmuramidase
-
-
-
-
Outer wedge of baseplate protein
-
-
-
-
P13
-
-
-
-
Peptidoglycan hydrolase
-
-
-
-
PR1-lysozyme
-
-
-
-
Protein gp17
-
-
-
-
Protein gp19
-
-
-
-
Protein Gp25
-
-
-
-
Protein Gp5
-
-
-
-
Protein gp54
-
-
-
-
Protein gpK
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis of O-glycosyl bond
-
-
-
-
SYSTEMATIC NAME
IUBMB Comments
peptidoglycan N-acetylmuramoylhydrolase
cf. also EC 3.2.1.14 chitinase.
CAS REGISTRY NUMBER
COMMENTARY hide
9001-63-2
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
-
-
Manually annotated by BRENDA team
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
-
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.
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
LYZ1_MOUSE
148
0
16794
Swiss-Prot
Secretory Pathway (Reliability: 1)
LYZ2_MOUSE
148
0
16689
Swiss-Prot
Secretory Pathway (Reliability: 1)
LYZL1_MOUSE
148
0
16802
Swiss-Prot
Secretory Pathway (Reliability: 2)
LYZL5_MOUSE
160
0
18005
Swiss-Prot
Secretory Pathway (Reliability: 1)
LYZL6_MOUSE
148
0
16818
Swiss-Prot
Secretory Pathway (Reliability: 2)
D3Z796_MOUSE
99
0
11504
TrEMBL
other Location (Reliability: 1)
A0A077S9N1_MOUSE
148
0
16794
TrEMBL
Secretory Pathway (Reliability: 1)
A0A077S2U6_MOUSE
148
0
16689
TrEMBL
Secretory Pathway (Reliability: 1)
A0A077S9Z4_MOUSE
148
0
16802
TrEMBL
Secretory Pathway (Reliability: 2)
OPRM_MOUSE
398
0
44421
Swiss-Prot
-
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Groebner, S.; Fritz, E.; Schoch, F.; Schaller, M.; Berger, A.C.; Bitzer, M.; Autenrieth, I.B.
Lysozyme activates Enterococcus faecium to induce necrotic cell death in macrophages
Cell. Mol. Life Sci.
67
3331-3344
2010
Mus musculus
Manually annotated by BRENDA team