Information on EC 6.3.2.1 - Pantoate-beta-alanine ligase:
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EC NUMBERCOMMENTARY
6.3.2.1-

RECOMMENDED NAMEGeneOntology No.
Pantoate-beta-alanine ligaseGO:0004592

REACTIONREACTION DIAGRAMCOMMENTARYORGANISM UNIPROT ACCESSION NO.LITERATURE
ATP + (R)-pantoate + beta-alanine = AMP + diphosphate + (R)-pantothenate
show the reaction diagram		----
ATP + (R)-pantoate + beta-alanine = AMP + diphosphate + (R)-pantothenate
show the reaction diagram		bi uni uni bi ping pong mechanismEscherichia coli-978

REACTION TYPEORGANISM UNIPROT ACCESSION NO.COMMENTARYLITERATURE
carboxamide formation----
carboxylic acid amide formation----
additional informationMycobacterium tuberculosis-pantothenate synthetase catalyzes the formation of a pantoyl-adenylate intermediate upon the ordered addition of ATP and pantoate650212

PATHWAYKEGG LinkMetaCyc Link
phosphopantothenate biosynthesis I-PANTO-PWY

SYSTEMATIC NAMEIUBMB Comments
(R)-Pantoate:beta-alanine ligase (AMP-forming)-

SYNONYMSORGANISM UNIPROT ACCESSION NO.COMMENTARYLITERATURE
D-Pantoate:beta-alanine ligase (AMP-forming)----
PanCMycobacterium tuberculosis--650029
PanCFusarium oxysporumQ96VJ9-653240
PanCMycobacterium tuberculosis-gene name714435
panthotenate synthetaseMycobacterium tuberculosis--653802
Pantoate activating enzyme----
Pantoic-activating enzyme----
Pantothenate synthetase----
Pantothenate synthetaseLotus japonicusO24035-649671
Pantothenate synthetaseOryza sativaO24210-649671
Pantothenate synthetaseEscherichia coli--653927, 694696, 716880
Pantothenate synthetaseMycobacterium tuberculosis--661144, 693541, 714435, 716880
Pantothenate synthetaseArabidopsis thalianaQ9FKB3-694696
Pantothenate synthetaseStaphylococcus aureusQ2FV22-714204
PSOryza sativaO24210-649671
PSMycobacterium tuberculosis--653802
PSEscherichia coli--653927
PTSArabidopsis thalianaQ9FKB3-694696
PTSEscherichia coli--694696
Synthetase, pantothenate----

CAS REGISTRY NUMBERCOMMENTARY
9023-49-8-

ORGANISMCOMMENTARYLITERATURESEQUENCE CODESEQUENCE DB SOURCE
Arabidopsis thaliana-663086, 674714--Manually annotated by BRENDA team
Arabidopsis thalianaecotype Columbia-0, single gene694696Q9FKB3UniProtManually annotated by BRENDA team
Brucella abortusstrain 19982--Manually annotated by BRENDA team
Brucella abortus 19strain 19982--Manually annotated by BRENDA team
Escherichia coli-653927, 663315, 674714, 716880, 975, 976, 978, 979, 981, 983--Manually annotated by BRENDA team
Escherichia coli-676279, 703685P31663UniProtManually annotated by BRENDA team
Escherichia coliB980--Manually annotated by BRENDA team
Escherichia coligene panC694696--Manually annotated by BRENDA team
Escherichia coliIFO 13168977--Manually annotated by BRENDA team
Fusarium oxysporumf. sp. lycopersici653240Q96VJ9SwissProtManually annotated by BRENDA team
Lotus japonicus-649671O24035SwissProtManually annotated by BRENDA team
Mycobacterium tuberculosis-650212, 653802, 661144, 674945, 714435, 716880--Manually annotated by BRENDA team
Mycobacterium tuberculosis-672114, 693541, 704206P0A5R0UniprotManually annotated by BRENDA team
Mycobacterium tuberculosisPanC is essential for growth650029--Manually annotated by BRENDA team
Oryza sativa-649671O24210SwissProtManually annotated by BRENDA team
Salmonella enterica subsp. enterica serovar Typhimurium-975--Manually annotated by BRENDA team
Staphylococcus aureus-714204Q2FV22UniProtManually annotated by BRENDA team

GENERAL INFORMATIONORGANISM UNIPROT ACCESSION NO.COMMENTARYLITERATURE
No entries in this field

SUBSTRATEPRODUCT                      REACTION DIAGRAMORGANISM UNIPROT ACCESSION NO. COMMENTARY/
Substrate		 LITERATURE/
Substrate		 COMMENTARY/
Product		 LITERATURE/
Product		 Reversibility
r=reversible
ir=irreversible
?=not specified
ATP + (R)-pantoate + beta-alanineAMP + diphosphate + (R)-pantothenate
show the reaction diagram		Salmonella enterica subsp. enterica serovar Typhimurium, Escherichia coli--975-975-
ATP + (R)-pantoate + beta-alanineAMP + diphosphate + (R)-pantothenate
show the reaction diagram		Escherichia coli--976-976-
ATP + (R)-pantoate + beta-alanineAMP + diphosphate + (R)-pantothenate
show the reaction diagram		Escherichia coli--977, 978, 979, 980, 981, 983---
ATP + (R)-pantoate + beta-alanineAMP + diphosphate + (R)-pantothenate
show the reaction diagram		Escherichia coli--653927-653927?
ATP + (R)-pantoate + beta-alanineAMP + diphosphate + (R)-pantothenate
show the reaction diagram		Escherichia coliP31663-676279--?
ATP + (R)-pantoate + beta-alanineAMP + diphosphate + (R)-pantothenate
show the reaction diagram		Escherichia coli--694696--?
ATP + (R)-pantoate + beta-alanineAMP + diphosphate + (R)-pantothenate
show the reaction diagram		Arabidopsis thaliana--663086--?
ATP + (R)-pantoate + beta-alanineAMP + diphosphate + (R)-pantothenate
show the reaction diagram		Brucella abortus--982---
ATP + (R)-pantoate + beta-alanineAMP + diphosphate + (R)-pantothenate
show the reaction diagram		Mycobacterium tuberculosis--650029-650029?
ATP + (R)-pantoate + beta-alanineAMP + diphosphate + (R)-pantothenate
show the reaction diagram		Mycobacterium tuberculosis--650212-650212?
ATP + (R)-pantoate + beta-alanineAMP + diphosphate + (R)-pantothenate
show the reaction diagram		Mycobacterium tuberculosis--653802-653802?
ATP + (R)-pantoate + beta-alanineAMP + diphosphate + (R)-pantothenate
show the reaction diagram		Mycobacterium tuberculosis--661144, 674945, 693541, 714435--?
ATP + (R)-pantoate + beta-alanineAMP + diphosphate + (R)-pantothenate
show the reaction diagram		Fusarium oxysporumQ96VJ9-653240-653240?
ATP + (R)-pantoate + beta-alanineAMP + diphosphate + (R)-pantothenate
show the reaction diagram		Lotus japonicusO24035-649671-649671?
ATP + (R)-pantoate + beta-alanineAMP + diphosphate + (R)-pantothenate
show the reaction diagram		Oryza sativaO24210-649671-649671?
ATP + (R)-pantoate + beta-alanineAMP + diphosphate + (R)-pantothenate
show the reaction diagram		Arabidopsis thalianaQ9FKB3-694696--?
ATP + (R)-pantoate + beta-alanineAMP + diphosphate + (R)-pantothenate
show the reaction diagram		Staphylococcus aureusQ2FV22-714204--?
ATP + (R)-pantoate + beta-alanineAMP + diphosphate + (R)-pantothenate
show the reaction diagram		Mycobacterium tuberculosis-last step in pantothenate biosynthesis pathway650029-650029?
ATP + (R)-pantoate + beta-alanineAMP + diphosphate + (R)-pantothenate
show the reaction diagram		Arabidopsis thaliana-the enzyme is involved in biosynthesis of the phosphopantetheine moiety663086--?
ATP + (R)-pantoate + beta-alanineAMP + diphosphate + (R)-pantothenate
show the reaction diagram		Escherichia coli, Arabidopsis thaliana-synthesis of pantothenate, the essential precursor to coenzyme A674714--?
ATP + (R)-pantoate + beta-alanineAMP + diphosphate + (R)-pantothenate
show the reaction diagram		Escherichia coli-Bi Uni Uni Bi kinetic mechanism. Enzyme displays non-allosteric behavior674714--?
ATP + (R)-pantoate + beta-alanineAMP + diphosphate + (R)-pantothenate
show the reaction diagram		Mycobacterium tuberculosisP0A5R0the phosphate group of AMP serves as an anchor for the binding of beta-alanine672114--?
ATP + (R)-pantoate + beta-alanineAMP + diphosphate + (R)-pantothenate
show the reaction diagram		Arabidopsis thaliana-the two-step reaction mechanism, large allosteric effects674714--?
ATP + (R)-pantoate + beta-alanine?
show the reaction diagram		Escherichia coli-formation of pantothenic acid, an important member of the B vitamins979---
CTP + (R)-pantoate + beta-alanineCMP + diphosphate + (R)-pantothenate
show the reaction diagram		Escherichia coli-14% of the activity relative to ATP978---
GTP + (R)-pantoate + beta-alanineGMP + diphosphate + (R)-pantothenate
show the reaction diagram		Escherichia coli-12% of the activity relative to ATP978---
UTP + (R)-pantoate + beta-alanineUMP + diphosphate + (R)-pantothenate
show the reaction diagram		Escherichia coli-16% of the activity relative to ATP978---
ITP + (R)-pantoate + beta-alanineIMP + diphosphate + (R)-pantothenate
show the reaction diagram		Escherichia coli-14% of the activity relative to ATP978---
additional information?-Arabidopsis thalianaQ9FKB3pantothenate synthetase is essential but not limiting for pantothenate biosynthesis in Arabidopsis thaliana, pantothenate, i.e. vitamin B5, is the universal precursor for coenzyme A, overview694696---

NATURAL SUBSTRATESNATURAL PRODUCTSREACTION DIAGRAMORGANISM UNIPROT ACCESSION NO.COMMENTARY SUBSTRATELITERATURE
(Substrate)		COMMENTARY PRODUCTLITERATURE
(Product)
ATP + (R)-pantoate + beta-alanineAMP + diphosphate + (R)-pantothenate
show the reaction diagram		Escherichia coli--653927-653927
ATP + (R)-pantoate + beta-alanineAMP + diphosphate + (R)-pantothenate
show the reaction diagram		Escherichia coli--694696--
ATP + (R)-pantoate + beta-alanineAMP + diphosphate + (R)-pantothenate
show the reaction diagram		Mycobacterium tuberculosis--650212-650212
ATP + (R)-pantoate + beta-alanineAMP + diphosphate + (R)-pantothenate
show the reaction diagram		Mycobacterium tuberculosis--653802-653802
ATP + (R)-pantoate + beta-alanineAMP + diphosphate + (R)-pantothenate
show the reaction diagram		Mycobacterium tuberculosis--693541--
ATP + (R)-pantoate + beta-alanineAMP + diphosphate + (R)-pantothenate
show the reaction diagram		Fusarium oxysporumQ96VJ9-653240-653240
ATP + (R)-pantoate + beta-alanineAMP + diphosphate + (R)-pantothenate
show the reaction diagram		Lotus japonicusO24035-649671-649671
ATP + (R)-pantoate + beta-alanineAMP + diphosphate + (R)-pantothenate
show the reaction diagram		Oryza sativaO24210-649671-649671
ATP + (R)-pantoate + beta-alanineAMP + diphosphate + (R)-pantothenate
show the reaction diagram		Arabidopsis thalianaQ9FKB3-694696--
ATP + (R)-pantoate + beta-alanineAMP + diphosphate + (R)-pantothenate
show the reaction diagram		Mycobacterium tuberculosis-last step in pantothenate biosynthesis pathway650029-650029
ATP + (R)-pantoate + beta-alanineAMP + diphosphate + (R)-pantothenate
show the reaction diagram		Arabidopsis thaliana-the enzyme is involved in biosynthesis of the phosphopantetheine moiety663086--
ATP + (R)-pantoate + beta-alanineAMP + diphosphate + (R)-pantothenate
show the reaction diagram		Escherichia coli, Arabidopsis thaliana-synthesis of pantothenate, the essential precursor to coenzyme A674714--
ATP + (R)-pantoate + beta-alanine?
show the reaction diagram		Escherichia coli-formation of pantothenic acid, an important member of the B vitamins979--
additional information?-Arabidopsis thalianaQ9FKB3pantothenate synthetase is essential but not limiting for pantothenate biosynthesis in Arabidopsis thaliana, pantothenate, i.e. vitamin B5, is the universal precursor for coenzyme A, overview694696--

COFACTORORGANISM UNIPROT ACCESSION NO.COMMENTARYLITERATUREIMAGE
ATPMycobacterium tuberculosis--693541 2D-image
ATPArabidopsis thalianaQ9FKB3-694696 2D-image
ATPEscherichia coli--694696 2D-image

METALS and IONS ORGANISM UNIPROT ACCESSION NO.COMMENTARY LITERATURE
Co2+Mycobacterium tuberculosis-maximal activity at 10 mM, slight activation650029
K+Escherichia coli-activates; Km: 5.5 mM977
K+Escherichia coli-combination of divalent and monovalent cation required978, 981
K+Escherichia coli-Km: 5.5 mM979
Mg2+Mycobacterium tuberculosis-maximal activity at 10 mM, very strong activation650029
Mg2+Mycobacterium tuberculosis--693541
Mg2+Arabidopsis thalianaQ9FKB3-694696
Mg2+Escherichia coli--694696
Mg2+Staphylococcus aureusQ2FV22-714204
Mg2+Escherichia coli-divalent cation required, Mg2+ or Mn2+, Km: 2.0 mM. Optimal concentration: 10 mM, inhibition above977, 978, 979
Mg2+Escherichia coli-combination of divalent and monovalent cation required981
Mg2+Brucella abortus-stimulates982
Mn2+Mycobacterium tuberculosis-maximal activity at 10 mM, very strong activation650029
Mn2+Escherichia coli-divalent cation required, Mg2+ or Mn2+. Optimal concentration: 5 mM, inhibition above977
Mn2+Escherichia coli-combination of divalent and monovalent cation required; divalent cation required, Mg2+ or Mn2+. Optimal concentration: 5 mM, inhibition above978
Mn2+Escherichia coli-combination of divalent and monovalent cation required981
NH4+Escherichia coli-activates977
NH4+Escherichia coli-combination of divalent and monovalent cation required978, 981
Ni2+Mycobacterium tuberculosis-maximal activity at approx. 3 mM, slight activation650029

INHIBITORSORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE IMAGE
(2RS)-5'-O-(2-hydroxy-4-methoxybutyrylsulfamoyl)adenosineEscherichia coli--676279 2D-image
(2RS)-5'-O-(3,3-dimethyl-2-aminobutyrylsulfamoyl)adenosineEscherichia coli--676279 2D-image
(2RS)-5'-O-(3,3-dimethyl-2-hydroxy-4-methoxybutyrylsulfamoyl)adenosineEscherichia coli--676279 2D-image
(2RS)-5'-O-(3,3-dimethyl-2-hydroxybutyrylsulfamoyl)adenosineEscherichia coli--676279 2D-image
(2RS)-5'-O-(3,3-dimethyl-2-oxobutyrylsulfamoyl)adenosineEscherichia coli--676279 2D-image
(2RS)-adenosyl-2-hydroxy-3,3-dimethylbuyrateEscherichia coli--676279 2D-image
(2RS)-adenosyl-2-hydroxy-4-methoxybutyrateEscherichia coli--676279 2D-image
(2RS)-adenosyl-3,3-dimethyl-2-hydroxy-4-methoxybutyrateEscherichia coli--676279 2D-image
(2S)-adenosyl-2-L-amino-3,3-dimethylbutanoateEscherichia coli--676279 2D-image
(R)-pantoateArabidopsis thaliana-substrate inhibition674714 2D-image
1,10-phenanthrolineEscherichia coli--977, 978, 979 2D-image
2,3-DiaminopropanoateEscherichia coli-slight978 2D-image
2-carboxybenzofuranoic acidMycobacterium tuberculosis-competitive with respect to both ATP and pantoate704206-
2-hydroxybutanoateEscherichia coli-slight978 2D-image
2-HydroxypropanoateEscherichia coli-slight978 2D-image
2-methyl-5-methoxyindoleMycobacterium tuberculosis-binding mode with the 2-CH3 group facing the pantoate pocket704206-
3,3-dimethyl-2-oxobutyric acid 5-(6-aminopurin-9-yl)-3,4-dihydroxytetrahydrofuran-2-ylmethyl esterEscherichia coli--676279 2D-image
3-hydroxybutanoateEscherichia coli-slight978 2D-image
3-hydroxypropanoateEscherichia coli-slight978 2D-image
4-(2-{3-[(1E,3E)-hexa-1,3,5-trien-1-yl]phenyl}hydrazinyl)-4-oxobutanoic acidMycobacterium tuberculosis-27% inhibition714435 2D-image
4-Amino-3-hydroxybutanoateEscherichia coli-32% inhibition at 1 mM977 2D-image
4-Amino-3-hydroxybutanoateEscherichia coli--978 2D-image
4-aminobutanoateEscherichia coli-27% inhibition at 1 mM977 2D-image
4-aminobutanoateEscherichia coli--978, 979 2D-image
4-[(4-[[(5-tert-butyl-4,5,6,7-tetrahydro-1,2-benzisoxazol-3-yl)carbonyl]amino]-1H-pyrazol-1-yl)methyl]benzoic acidMycobacterium tuberculosis-0.1 mM, 99% inhibition693541 2D-image
5-AminopentanoateEscherichia coli-slight978 2D-image
5-AminopentanoateEscherichia coli--979 2D-image
5-methoxyindoleMycobacterium tuberculosis-competitive with respect to ATP704206 2D-image
5-tert-butyl-4,5,6,7-tetrahydro-1,2-benzisoxazole-3-carboxylic acidMycobacterium tuberculosis-0.1 mM, 12% inhibition693541 2D-image
5-tert-butyl-N-(1-[4-[(2-phenylethyl)carbamoyl]benzyl]-1H-pyrazol-4-yl)-4,5,6,7-tetrahydro-1,2-benzisoxazole-3-carboxamideMycobacterium tuberculosis-0.1 mM, 78% inhibition693541 2D-image
5-tert-butyl-N-1H-pyrazol-4-yl-4,5,6,7-tetrahydro-1,2-benzisoxazole-3-carboxamideMycobacterium tuberculosis-0.1 mM, 43% inhibition693541 2D-image
5-tert-butyl-N-pyrazol-4-yl-4,5,6,7-tetrahydrobenzo[d]isoxazole-3-carboxamide derivativesMycobacterium tuberculosis-silico molecular design, synthesis, and inhibitory activity, overview693541 2D-image
5-tert-butyl-N-[1-(2,4,6-trichlorophenyl)-1H-pyrazol-4-yl]-4,5,6,7-tetrahydro-1,2-benzisoxazole-3-carboxamideMycobacterium tuberculosis-0.1 mM, 17% inhibition693541 2D-image
5-tert-butyl-N-[1-(2,4-difluorobenzyl)-1H-pyrazol-4-yl]-4,5,6,7-tetrahydro-1,2-benzisoxazole-3-carboxamideMycobacterium tuberculosis-0.1 mM, 100% inhibition693541 2D-image
5-tert-butyl-N-[1-(2-iodobenzyl)-1H-pyrazol-4-yl]-4,5,6,7-tetrahydro-1,2-benzisoxazole-3-carboxamideMycobacterium tuberculosis-0.1 mM, 84% inhibition693541 2D-image
5-tert-butyl-N-[1-(2-methylbenzyl)-1H-pyrazol-4-yl]-4,5,6,7-tetrahydro-1,2-benzisoxazole-3-carboxamideMycobacterium tuberculosis-0.1 mM, 89% inhibition693541 2D-image
5-tert-butyl-N-[1-(4-chlorobenzyl)-1H-pyrazol-4-yl]-4,5,6,7-tetrahydro-1,2-benzisoxazole-3-carboxamideMycobacterium tuberculosis-0.1 mM, 98% inhibition693541 2D-image
5-tert-butyl-N-[1-(4-fluorobenzyl)-1H-pyrazol-4-yl]-4,5,6,7-tetrahydro-1,2-benzisoxazole-3-carboxamideMycobacterium tuberculosis-0.1 mM, 98% inhibition693541 2D-image
5-tert-butyl-N-[1-(naphthalen-2-ylmethyl)-1H-pyrazol-4-yl]-4,5,6,7-tetrahydro-1,2-benzisoxazole-3-carboxamideMycobacterium tuberculosis-0.1 mM, 97% inhibition693541 2D-image
5-tert-butyl-N-[4-carbamoyl-3-(4-methoxybenzyl)isoxazol-5-yl]-4,5,6,7-tetrahydro-1,2-benzisoxazole-3-carboxamideMycobacterium tuberculosis-0.1 mM, 79% inhibition693541 2D-image
6-AminohexanoateEscherichia coli-slight978 2D-image
actinomycin DMycobacterium tuberculosis--714435 2D-image
Ag+Escherichia coli--977, 978, 979 2D-image
AMPEscherichia coli--979 2D-image
anserineEscherichia coli-slight978 2D-image
AspEscherichia coli-uncompetitive979 2D-image
aspartateEscherichia coli-24% inhibition at 1 mM977 2D-image
Ba2+Escherichia coli--977, 978 2D-image
Ca2+Escherichia coli--977, 978, 979 2D-image
carnosineEscherichia coli-slight978 2D-image
Co2+Escherichia coli--977, 978 2D-image
Cu2+Escherichia coli--977, 978, 979 2D-image
cysteineEscherichia coli-weak979 2D-image
diphosphateEscherichia coli--979 2D-image
DTTEscherichia coli-weak979 2D-image
EDTAEscherichia coli--977, 978 2D-image
EGTAEscherichia coli--977, 978 2D-image
Fe2+Escherichia coli-slight977 2D-image
Fe2+Escherichia coli--978, 979 2D-image
gluconateEscherichia coli-32% inhibition at 1 mM977, 978 2D-image
glycolateEscherichia coli-30% inhibition at 1 mM977, 978 2D-image
Hg2+Escherichia coli--977, 978, 979 2D-image
iodoacetateEscherichia coli--978 2D-image
iodoacetateEscherichia coli-weak979 2D-image
L-AlaEscherichia coli--978, 979 2D-image
L-cysteateEscherichia coli--978 2D-image
L-ValEscherichia coli--978 2D-image
L-ValEscherichia coli-uncompetitive979 2D-image
LactateEscherichia coli--978 2D-image
Li+Escherichia coli--979 2D-image
mercaptoethanolEscherichia coli-weak979 2D-image
MercaptoethanolamineEscherichia coli-weak979 2D-image
MercaptopurineEscherichia coli-weak979 2D-image
methyl 4-[(4-[[(5-tert-butyl-4,5,6,7-tetrahydro-1,2-benzisoxazol-3-yl)carbonyl]amino]-1H-pyrazol-1-yl)methyl]benzoateMycobacterium tuberculosis-0.1 mM, 100% inhibition693541 2D-image
methyl 6-amino-4-(benzyloxy)-1H-indole-2-carboxylateMycobacterium tuberculosis-69% inhibition714435 2D-image
MethylmalonateEscherichia coli-38% inhibition at 1 mM977 2D-image
Mg2+Escherichia coli-inhibition above 10 mM977 2D-image
Mn2+Escherichia coli-inhibition above 5 mM977 2D-image
N-(1-benzyl-1H-pyrazol-4-yl)-5-tert-butyl-4,5,6,7-tetrahydro-1,2-benzisoxazole-3-carboxamideMycobacterium tuberculosis-0.1 mM, 100% inhibition693541 2D-image
N-(2,5-dibromophenyl)-2-hydroxybenzamideMycobacterium tuberculosis--693541 2D-image
N-[1-(2,4-dichlorobenzyl)-1H-pyrazol-4-yl]-4,5,6,7-tetrahydro-1,2-benzisoxazole-3-carboxamideMycobacterium tuberculosis-0.1 mM, 18% inhibition693541 2D-image
N-[1-(2-bromobenzyl)-1H-pyrazol-4-yl]-5-tert-butyl-4,5,6,7-tetrahydro-1,2-benzisoxazole-3-carboxamideMycobacterium tuberculosis-0.1 mM, 94% inhibition693541 2D-image
N-[1-[4-(benzylcarbamoyl)benzyl]-1H-pyrazol-4-yl]-5-tert-butyl-4,5,6,7-tetrahydro-1,2-benzisoxazole-3-carboxamideMycobacterium tuberculosis-0.1 mM, 82% inhibition693541 2D-image
nafronyl oxalateMycobacterium tuberculosis-competitive inhibitor674945 2D-image
nafronyl oxalateMycobacterium tuberculosis--714435 2D-image
Ni2+Escherichia coli-slight977, 978 2D-image
Ni2+Escherichia coli--979 2D-image
pantothenateMycobacterium tuberculosis-product inhibition650029 2D-image
pantothenic acidEscherichia coli--979 2D-image
Pb2+Escherichia coli-slight977 2D-image
Pb2+Escherichia coli--979 2D-image
PCMBEscherichia coli--979 2D-image
Sn2+Escherichia coli-slight977, 978 2D-image
Sr2+Escherichia coli-slight977, 978 2D-image
TaurineEscherichia coli-52% inhibition at 1 mM977 2D-image
TaurineEscherichia coli--978, 979 2D-image
tert-butyl 4-[(4-[[(5-tert-butyl-4,5,6,7-tetrahydro-1,2-benzisoxazol-3-yl)carbonyl]amino]-1H-pyrazol-1-yl)methyl]benzoateMycobacterium tuberculosis-0.1 mM, 79% inhibition693541 2D-image
Zn2+Escherichia coli--977, 978, 979 2D-image

ACTIVATING COMPOUNDORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE IMAGE
additional informationFusarium oxysporumQ96VJ9PanC expression is induced by alpha-tomatine653240-

KM VALUE [mM]KM VALUE [mM] MaximumSUBSTRATEORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE IMAGE
0.41-(R)-pantoateMycobacterium tuberculosis--674945 2D-image
1.45-(R)-pantoateEscherichia coli-25°C676279 2D-image
0.091-ATPEscherichia coli--979 2D-image
0.1-ATPEscherichia coli--653927, 977, 978 2D-image
1.75-ATPEscherichia coli-25°C676279 2D-image
2.6-ATPMycobacterium tuberculosis-25°C, pH 7.8650029 2D-image
0.04-beta-AlanineBrucella abortus--982 2D-image
0.056-beta-AlanineEscherichia coli--981 2D-image
0.09-beta-AlanineMycobacterium tuberculosis-25°C, pH 7.8, mutant enzyme K160C661144 2D-image
0.15-beta-AlanineEscherichia coli--653927, 977, 978 2D-image
0.27-beta-AlanineMycobacterium tuberculosis-25°C, pH 7.8, wild-type enzyme661144 2D-image
0.3-beta-AlanineMycobacterium tuberculosis-25°C, pH 7.8, mutant enzyme Q164A661144 2D-image
0.31-beta-AlanineEscherichia coli-25°C676279 2D-image
0.44-beta-AlanineLotus japonicusO2403525°C, pH 8.0, at 20 mM pantoate649671 2D-image
0.8-beta-AlanineMycobacterium tuberculosis-25°C, pH 7.8650029 2D-image
0.98-beta-AlanineLotus japonicusO2403525°C, pH 8.0, at 0.5 mM pantoate649671 2D-image
0.063-D-pantoateEscherichia coli--977, 978 2D-image
0.063-D-pantoateEscherichia coli-beta-alanine979 2D-image
0.13-D-pantoateMycobacterium tuberculosis-25°C, pH 7.8650029 2D-image
0.044-PantoateLotus japonicusO2403525°C, pH 8.0649671 2D-image
0.063-PantoateEscherichia coli--653927 2D-image
0.12-PantoateEscherichia coli--979, 981 2D-image
50-PantoateBrucella abortus--982 2D-image

TURNOVER NUMBER [1/s] TURNOVER NUMBER MAXIMUM[1/s] SUBSTRATEORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE IMAGE
0.039-(R)-pantoateArabidopsis thaliana-25°C, pH 8.0, wild-type enzyme674714 2D-image
0.81-(R)-pantoateArabidopsis thaliana-25°C, pH 8.0, mutant enzyme E132A674714 2D-image
1.4-(R)-pantoateEscherichia coli-25°C676279 2D-image
1.5-(R)-pantoateStaphylococcus aureusQ2FV22co-substrate: beta-alanine, pH 8.0, 30°C714204 2D-image
1.4-ATPEscherichia coli-25°C676279 2D-image
0.01-beta-AlanineMycobacterium tuberculosis-25°C, pH 7.8, mutant enzyme K160C661144 2D-image
0.02-beta-AlanineMycobacterium tuberculosis-25°C, pH 7.8, mutant enzyme Q164A661144 2D-image
0.16-beta-AlanineArabidopsis thaliana-25°C, pH 8.0, wild-type enzyme674714 2D-image
0.59-beta-AlanineArabidopsis thaliana-25°C, pH 8.0, mutant enzyme E132A674714 2D-image
1.01-beta-AlanineMycobacterium tuberculosis-25°C, pH 7.8, wild-type enzyme661144 2D-image
1.4-beta-AlanineEscherichia coli-25°C676279 2D-image
1.5-beta-AlanineStaphylococcus aureusQ2FV22co-substrate: (R)-pantoate, pH 8.0, 30°C714204 2D-image
3.4-beta-AlanineMycobacterium tuberculosis-25°C, pH 7.8650029 2D-image
3.4-D-pantoateMycobacterium tuberculosis-25°C, pH 7.8650029 2D-image
0.62-PantoateLotus japonicusO2403525°C, pH 8.0649671 2D-image
1.74-PantoateMycobacterium tuberculosis--653802 2D-image
2.94-PantoateMycobacterium tuberculosis--653802 2D-image
6.08-PantoateLotus japonicusO2403525°C, pH 8.0649671 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
0.0008-(2RS)-5'-O-(2-hydroxy-4-methoxybutyrylsulfamoyl) adenosineEscherichia coli-25°C676279 2D-image
0.065-(2RS)-5'-O-(3,3-dimethyl-2-aminobutyrylsulfamoyl)adenosineEscherichia coli-25°C676279 2D-image
0.16-(2RS)-5'-O-(3,3-dimethyl-2-aminobutyrylsulfamoyl)adenosineEscherichia coli-25°C676279 2D-image
0.25-(2RS)-5'-O-(3,3-dimethyl-2-aminobutyrylsulfamoyl)adenosineEscherichia coli-25°C676279 2D-image
0.03-(2RS)-5'-O-(3,3-dimethyl-2-hydroxy-4-methoxybutyrylsulfamoyl)adenosineEscherichia coli-25°C676279 2D-image
0.054-(2RS)-5'-O-(3,3-dimethyl-2-hydroxy-4-methoxybutyrylsulfamoyl)adenosineEscherichia coli-25°C676279 2D-image
0.144-(2RS)-5'-O-(3,3-dimethyl-2-hydroxy-4-methoxybutyrylsulfamoyl)adenosineEscherichia coli-25°C676279 2D-image
0.0003-(2RS)-5'-O-(3,3-dimethyl-2-hydroxybutyrylsulfamoyl)adenosineEscherichia coli-25°C676279 2D-image
0.0008-(2RS)-5'-O-(3,3-dimethyl-2-hydroxybutyrylsulfamoyl)adenosineEscherichia coli-25°C676279 2D-image
0.0011-(2RS)-5'-O-(3,3-dimethyl-2-hydroxybutyrylsulfamoyl)adenosineEscherichia coli-25°C676279 2D-image
0.014-(2RS)-5'-O-(3,3-dimethyl-2-oxobutyrylsulfamoyl)adenosineEscherichia coli-25°C676279 2D-image
0.015-(2RS)-5'-O-(3,3-dimethyl-2-oxobutyrylsulfamoyl)adenosineEscherichia coli-25°C676279 2D-image
0.12-(2RS)-5'-O-(3,3-dimethyl-2-oxobutyrylsulfamoyl)adenosineEscherichia coli-25°C676279 2D-image
2.5-(2RS)-adenosyl-2-hydroxy-3,3-dimethylbuyrateEscherichia coli-25°C676279 2D-image
3.5-(2RS)-adenosyl-2-hydroxy-4-methoxybutyrateEscherichia coli-25°C676279 2D-image
18.2-(2RS)-adenosyl-3,3-dimethyl-2-hydroxy-4-methoxybutyrateEscherichia coli-25°C676279 2D-image
9.5-(2S)-adenosyl-2-L-amino-3,3-dimethylbutanoateEscherichia coli-25°C676279 2D-image
1.9-3,3-dimethyl-2-oxobutyric acid 5-(6-aminopurin-9-yl)-3,4-dihydroxytetrahydrofuran-2-ylmethyl esterEscherichia coli-25°C676279 2D-image
0.075-nafronyl oxalateMycobacterium tuberculosis--674945 2D-image
4.5-pantothenateMycobacterium tuberculosis-25°C, pH 7.8, vs. beta-alanine650029 2D-image
5.7-pantothenateMycobacterium tuberculosis-25°C, pH 7.8, vs. D-pantoate650029 2D-image
7.6-pantothenateMycobacterium tuberculosis-25°C, pH 7.8, vs. ATP650029 2D-image

IC50 VALUE [mM]IC50 VALUE [mM] MaximumINHIBITORORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE IMAGE
460-4-[(4-[[(5-tert-butyl-4,5,6,7-tetrahydro-1,2-benzisoxazol-3-yl)carbonyl]amino]-1H-pyrazol-1-yl)methyl]benzoic acidMycobacterium tuberculosis--693541 2D-image
140-5-tert-butyl-N-(1-[4-[(2-phenylethyl)carbamoyl]benzyl]-1H-pyrazol-4-yl)-4,5,6,7-tetrahydro-1,2-benzisoxazole-3-carboxamideMycobacterium tuberculosis--693541 2D-image
61000-5-tert-butyl-N-1H-pyrazol-4-yl-4,5,6,7-tetrahydro-1,2-benzisoxazole-3-carboxamideMycobacterium tuberculosis--693541 2D-image
130-5-tert-butyl-N-[1-(2,4-difluorobenzyl)-1H-pyrazol-4-yl]-4,5,6,7-tetrahydro-1,2-benzisoxazole-3-carboxamideMycobacterium tuberculosis--693541 2D-image
160-5-tert-butyl-N-[1-(2-iodobenzyl)-1H-pyrazol-4-yl]-4,5,6,7-tetrahydro-1,2-benzisoxazole-3-carboxamideMycobacterium tuberculosis--693541 2D-image
120-5-tert-butyl-N-[1-(2-methylbenzyl)-1H-pyrazol-4-yl]-4,5,6,7-tetrahydro-1,2-benzisoxazole-3-carboxamideMycobacterium tuberculosis--693541 2D-image
140-5-tert-butyl-N-[1-(4-chlorobenzyl)-1H-pyrazol-4-yl]-4,5,6,7-tetrahydro-1,2-benzisoxazole-3-carboxamideMycobacterium tuberculosis--693541 2D-image
150-5-tert-butyl-N-[1-(4-fluorobenzyl)-1H-pyrazol-4-yl]-4,5,6,7-tetrahydro-1,2-benzisoxazole-3-carboxamideMycobacterium tuberculosis--693541 2D-image
90-5-tert-butyl-N-[1-(naphthalen-2-ylmethyl)-1H-pyrazol-4-yl]-4,5,6,7-tetrahydro-1,2-benzisoxazole-3-carboxamideMycobacterium tuberculosis--693541 2D-image
7130-5-tert-butyl-N-[4-carbamoyl-3-(4-methoxybenzyl)isoxazol-5-yl]-4,5,6,7-tetrahydro-1,2-benzisoxazole-3-carboxamideMycobacterium tuberculosis--693541 2D-image
0.2507-actinomycin DMycobacterium tuberculosis-pH and temperature not specified in the publication714435 2D-image
160-methyl 4-[(4-[[(5-tert-butyl-4,5,6,7-tetrahydro-1,2-benzisoxazol-3-yl)carbonyl]amino]-1H-pyrazol-1-yl)methyl]benzoateMycobacterium tuberculosis--693541 2D-image
0.02244-methyl 6-amino-4-(benzyloxy)-1H-indole-2-carboxylateMycobacterium tuberculosis-pH and temperature not specified in the publication714435 2D-image
97-N-(1-benzyl-1H-pyrazol-4-yl)-5-tert-butyl-4,5,6,7-tetrahydro-1,2-benzisoxazole-3-carboxamideMycobacterium tuberculosis--693541 2D-image
140-N-[1-(2-bromobenzyl)-1H-pyrazol-4-yl]-5-tert-butyl-4,5,6,7-tetrahydro-1,2-benzisoxazole-3-carboxamideMycobacterium tuberculosis--693541 2D-image
210-N-[1-[4-(benzylcarbamoyl)benzyl]-1H-pyrazol-4-yl]-5-tert-butyl-4,5,6,7-tetrahydro-1,2-benzisoxazole-3-carboxamideMycobacterium tuberculosis--693541 2D-image
0.3984-nafronyl oxalateMycobacterium tuberculosis-pH and temperature not specified in the publication714435 2D-image
250-tert-butyl 4-[(4-[[(5-tert-butyl-4,5,6,7-tetrahydro-1,2-benzisoxazol-3-yl)carbonyl]amino]-1H-pyrazol-1-yl)methyl]benzoateMycobacterium tuberculosis--693541 2D-image

SPECIFIC ACTIVITY [µmol/min/mg] SPECIFIC ACTIVITY MAXIMUM ORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE
1.36-Lotus japonicusO24035-649671
2.05-Escherichia coli--977, 980

pH OPTIMUMpH MAXIMUMORGANISM UNIPROT ACCESSION NO. COMMENTARYLITERATURE
5.5-Arabidopsis thaliana, Escherichia coli-exchange between beta-alanine and pantothenate in the presence of AMP674714
7.8-Lotus japonicusO24035in Tris-HCl649671
88.5Brucella abortus--982
8-Lotus japonicusO24035in potassium phosphate649671
8.5-Staphylococcus aureusQ2FV22-714204
9-Arabidopsis thaliana, Escherichia coli-synthesis of pantothenate674714
9-Arabidopsis thalianaQ9FKB3assay at694696
9-Escherichia coli-assay at694696
10-Escherichia coli--653927, 978, 979

pH RANGEpH RANGE MAXIMUMORGANISM UNIPROT ACCESSION NO.COMMENTARYLITERATURE
69Lotus japonicusO2403550% of maximal activity at pH 7.0, 15% of maximal activity at pH 6.0 and pH 9.0 respectively649671
7.19Lotus japonicusO24035in Tris-HCl, no activity at pH 7.0, 75% of maximal activity at pH 9.0649671
7.49.4Brucella abortus-7.4: about 40% of maximal activity, 9.4: about 80% of maximal activity982
812Escherichia coli-about 50% of maximal activity at pH 8 and 12979
89Staphylococcus aureusQ2FV22-714204

TEMPERATURE OPTIMUMTEMPERATURE OPTIMUM MAXIMUMORGANISM UNIPROT ACCESSION NO.COMMENTARYLITERATURE
30-Staphylococcus aureusQ2FV22-714204
30-Escherichia coli--978, 979, 981

TEMPERATURE RANGE TEMPERATURE MAXIMUM ORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE
2050Escherichia coli-20°C: about 60% of maximal activity, 50°C, about 25% of maximal activity979
3045Escherichia coli-30°C: maximal activity, 37°C: 90% of maximal activity, 45°C: 60% of maximal activity981

pI VALUEpI VALUE MAXIMUMORGANISM UNIPROT ACCESSION NO.COMMENTARYLITERATURE
No entries in this field

SOURCE TISSUE ORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE SOURCE
leafArabidopsis thalianaQ9FKB3-694696Manually annotated by BRENDA team
seedArabidopsis thalianaQ9FKB3transcript and metabolite patterns of CoA biosynthesis during seed development involving the enzyme, overview694696Manually annotated by BRENDA team

LOCALIZATION ORGANISM UNIPROT ACCESSION NO. COMMENTARY GeneOntology No. LITERATURE SOURCE
cytosolLotus japonicusO24035-5829649671Manually annotated by BRENDA team
cytosolArabidopsis thaliana--5829663086Manually annotated by BRENDA team

PDBSCOPCATHORGANISM
2ir7, downloadSCOP (2ir7)CATH (2ir7)Aquifex aeolicus (strain VF5)
3inn, downloadSCOP (3inn)CATH (3inn)Brucella melitensis biotype 1 (strain 16M / ATCC 23456 / NCTC 10094)
3uk2, downloadSCOP (3uk2)CATH (3uk2)Burkholderia thailandensis (strain E264 / ATCC 700388 / DSM 13276 / CIP 106301)
3mxt, downloadSCOP (3mxt)CATH (3mxt)Campylobacter jejuni subsp. jejuni serotype O:2 (strain NCTC 11168)
3uy4, downloadSCOP (3uy4)CATH (3uy4)Campylobacter jejuni subsp. jejuni serotype O:2 (strain NCTC 11168)
1iho, downloadSCOP (1iho)CATH (1iho)Escherichia coli (strain K12)
3guz, downloadSCOP (3guz)CATH (3guz)Escherichia coli (strain K12)
3n8h, downloadSCOP (3n8h)CATH (3n8h)Francisella tularensis subsp. tularensis (strain SCHU S4 / Schu 4)
3qtt, downloadSCOP (3qtt)CATH (3qtt)Francisella tularensis subsp. tularensis (strain SCHU S4 / Schu 4)
1mop, downloadSCOP (1mop)CATH (1mop)Mycobacterium tuberculosis
1n2b, downloadSCOP (1n2b)CATH (1n2b)Mycobacterium tuberculosis
1n2e, downloadSCOP (1n2e)CATH (1n2e)Mycobacterium tuberculosis
1n2g, downloadSCOP (1n2g)CATH (1n2g)Mycobacterium tuberculosis
1n2h, downloadSCOP (1n2h)CATH (1n2h)Mycobacterium tuberculosis
1n2i, downloadSCOP (1n2i)CATH (1n2i)Mycobacterium tuberculosis
1n2j, downloadSCOP (1n2j)CATH (1n2j)Mycobacterium tuberculosis
1n2o, downloadSCOP (1n2o)CATH (1n2o)Mycobacterium tuberculosis
2a7x, downloadSCOP (2a7x)CATH (2a7x)Mycobacterium tuberculosis
2a84, downloadSCOP (2a84)CATH (2a84)Mycobacterium tuberculosis
2a86, downloadSCOP (2a86)CATH (2a86)Mycobacterium tuberculosis
2a88, downloadSCOP (2a88)CATH (2a88)Mycobacterium tuberculosis
3cov, downloadSCOP (3cov)CATH (3cov)Mycobacterium tuberculosis
3cow, downloadSCOP (3cow)CATH (3cow)Mycobacterium tuberculosis
3coy, downloadSCOP (3coy)CATH (3coy)Mycobacterium tuberculosis
3coz, downloadSCOP (3coz)CATH (3coz)Mycobacterium tuberculosis
3imc, downloadSCOP (3imc)CATH (3imc)Mycobacterium tuberculosis
3ime, downloadSCOP (3ime)CATH (3ime)Mycobacterium tuberculosis
3img, downloadSCOP (3img)CATH (3img)Mycobacterium tuberculosis
3iob, downloadSCOP (3iob)CATH (3iob)Mycobacterium tuberculosis
3ioc, downloadSCOP (3ioc)CATH (3ioc)Mycobacterium tuberculosis
3iod, downloadSCOP (3iod)CATH (3iod)Mycobacterium tuberculosis
3ioe, downloadSCOP (3ioe)CATH (3ioe)Mycobacterium tuberculosis
3isj, downloadSCOP (3isj)CATH (3isj)Mycobacterium tuberculosis
3iub, downloadSCOP (3iub)CATH (3iub)Mycobacterium tuberculosis
3iue, downloadSCOP (3iue)CATH (3iue)Mycobacterium tuberculosis
3ivc, downloadSCOP (3ivc)CATH (3ivc)Mycobacterium tuberculosis
3ivg, downloadSCOP (3ivg)CATH (3ivg)Mycobacterium tuberculosis
3ivx, downloadSCOP (3ivx)CATH (3ivx)Mycobacterium tuberculosis
3le8, downloadSCOP (3le8)CATH (3le8)Mycobacterium tuberculosis
3mue, downloadSCOP (3mue)CATH (3mue)Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
2x3f, downloadSCOP (2x3f)CATH (2x3f)Staphylococcus aureus (strain MRSA252)
3ag5, downloadSCOP (3ag5)CATH (3ag5)Staphylococcus aureus (strain NCTC 8325)
3ag6, downloadSCOP (3ag6)CATH (3ag6)Staphylococcus aureus (strain NCTC 8325)
2ejc, downloadSCOP (2ejc)CATH (2ejc)Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099)
1ufv, downloadSCOP (1ufv)CATH (1ufv)Thermus thermophilus (strain HB8 / ATCC 27634 / DSM 579)
1v8f, downloadSCOP (1v8f)CATH (1v8f)Thermus thermophilus (strain HB8 / ATCC 27634 / DSM 579)
3q10, downloadSCOP (3q10)CATH (3q10)Yersinia pestis
3q12, downloadSCOP (3q12)CATH (3q12)Yersinia pestis

MOLECULAR WEIGHT MOLECULAR WEIGHT MAXIMUM ORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE
65000-Mycobacterium tuberculosis-gel filtration650029
65000-Escherichia coli-gel filtration653927
69000-Escherichia coli-gel filtration977, 979, 980
70000-Escherichia coli-sedimentation equilibrium ultracentrifugation977, 980
72800-Lotus japonicusO24035gel filtration649671

SUBUNITS ORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE
?Oryza sativaO24210x * 33900, deduced from nucleotide sequence649671
?Fusarium oxysporumQ96VJ9x * 43000, SDS-PAGE653240
?Escherichia coli-x * 18000, SDS-PAGE in presence of 2-mercaptoethanol977, 980
dimerLotus japonicusO240352 * 34000, SDS-PAGE649671
dimerMycobacterium tuberculosis-2 * 32677, deduced from nucleotide sequence; 2 * 33000, SDS-PAGE650029
dimerMycobacterium tuberculosis-2 * 31611, mass spectroscopy, crystallization653802
dimerEscherichia coli-2 * 30000, SDS-PAGE653927
dimerArabidopsis thaliana, Escherichia coli--674714
dimerEscherichia coli, Mycobacterium tuberculosis-molecular dynamics simulations show that the functional dynamics of the enzyme are dominated by motions of a flexible gate loop in the N-terminal domain and of the C-terminal domain. The gate loop motions dominate in Mycobacterium tuberculosis pantothenate synthetase while the C-terminal domain motion dominates in Escherichia coli pantothenate synthetase. Simulations also show that the correlated motions of the domains are severely compromised in the monomeric forms716880

POSTTRANSLATIONAL MODIFICATION ORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE
No entries in this field

Crystallization/COMMENTARY ORGANISM UNIPROT ACCESSION NO. LITERATURE
crystal structures of pantothenate synthetase complexed with diphosphomethylphosphonic acid adenosyl ester and pantoate resolved at 1.6 A and of apo Escherichia coli pantothenate synthetase resolved at 1.70 A are used as the initial structures for the simulationsEscherichia coli-716880
native and selenomethionine labeled PS, hanging drop vapor diffusion, hanging drops are composed of equal volumes of PS and reservoir solutions consisting of 50 mM Tris-HCl, pH 8.0, 4%-6% polyethylene glycol 4000, crystals appeare at 19°C after 2-4 days, crystals diffract to 1.7 AEscherichia coli-653927
tertiary structure of the dimeric N-terminal domain of Escherichia coli pantothenate synthetase, to a resolution of 1.7 A, shows a second molecule of pantoate bound in the ATP-binding pocket. Pantoate binding to the ATP-binding site induces large changes in structure, mainly for backbone and side chain atoms of residues in the ATP binding HXGH(34-37) motif. ATP stoichiometrically displaces pantoate from the ATP-binding siteEscherichia coli-703685
crystal structure of the enzyme complexed with AMP, ATP or beta-alanineMycobacterium tuberculosis-672114
crystal structures of pantothenate synthetase complexed with diphosphomethylphosphonic acid adenosyl ester and pantoate resolved at 1.6 A and of apo Escherichia coli pantothenate synthetase resolved at 1.70 A are used as the initial structures for the simulationsMycobacterium tuberculosis-716880
crystal structures with compounds 5-methoxyindole and 2-carboxybenzofuranoic acid bound in a ternary complex and in complex with 2-(2-((benzofuran-2-carboxamido)methyl)-5-methoxy-1H-indol-1-yl)acetic acidMycobacterium tuberculosis-704206
crystals of native PS and PS complexed with alpha,beta-methyleneadenosine 5'-triphosphate, pantoate and the reaction intermediate pantoyl adenylate, crystals are grown by hanging-drop vapor diffusion, 0.003-0.005 ml of PS solution at 10 mg/ml PS is mixed with an equal volume of well solution, best crystals are obtained with well solutions containing 10%-15% polyethylene glycol 3000, 5% glycerol, 2% ethanol, 20 mM MgCl2, 150 mM Li2SO4 and 100 mM imidazole, pH 8.0 at 20°C, crystals diffract to 1.6-2.0 AMycobacterium tuberculosis-653802
structures of the apoenzyme and the reaction intermediate complex are determined by X-ray crystallography to resolutions of 2.5 A and 1.85 A, respectively. Structural analysis indicate that the apoenzyme adopts an open and relatively mobile structure, while the complex structure is closed and entirely rigid. In the complex structure, pantothenate synthetase and acetate are bound in the active site. Acetate might mimic the substrate beta-alanine. Therefore, the complex structure might represent a catalytic state poised for in-line nucleophilic attack on pantothenate synthetaseStaphylococcus aureusQ2FV22714204

pH STABILITYpH STABILITY MAXIMUM ORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE
511Escherichia coli-15 min, 40°C, stable978

TEMPERATURE STABILITYTEMPERATURE STABILITY MAXIMUM ORGANISM UNIPROT ACCESSION NO. COMMENTARYLITERATURE
37-Escherichia coli-pH 5.0-10.0, 15 min stable977, 979
60-Escherichia coli-10 min, complete loss of activity978

GENERAL STABILITYORGANISM UNIPROT ACCESSION NO.LITERATURE
lyophilized enzyme is very stableEscherichia coli-977, 978

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
-20°C, stable for 6 monthsEscherichia coli-977, 978
-20°C, no loss of activityLotus japonicusO24035649671
4°C, 4 weeks, 25% loss of activityLotus japonicusO24035649671

Purification/COMMENTARY ORGANISM UNIPROT ACCESSION NO. LITERATURE
-Arabidopsis thaliana-674714
-Escherichia coli-674714, 977, 980
fusion protein with cytochrome b5Escherichia coli-663315
partialEscherichia coli-979
recombinant His-tagged enzymeEscherichia coli-694696
recombinant pantothenate synthetaseEscherichia coli-653927
recombinant PanCFusarium oxysporumQ96VJ9653240
recombinant pantothenate snthetaseLotus japonicusO24035649671
-Mycobacterium tuberculosis-661144
recombinant PanCMycobacterium tuberculosis-650029
recombinant pantothenate synthetaseMycobacterium tuberculosis-650212
recombinant PSMycobacterium tuberculosis-653802
using Ni-NTA chromatographyStaphylococcus aureusQ2FV22714204

Cloned/COMMENTARY ORGANISM UNIPROT ACCESSION NO. LITERATURE
-Arabidopsis thaliana-663086
expression in Escherichia coli as N-terminal His-tagged proteinArabidopsis thaliana-674714
promoter:beta-glucuronidase analysisArabidopsis thalianaQ9FKB3694696
-Escherichia coli-653927
expression in Escherichia coli BL21 as N-terminal His-tagged proteinEscherichia coli-674714
gene panC, recombinant expression as His-tagged enzyme, and expression in and complementation of the Arabidopsis thaliana knockout mutant phenotype by heterologous expression of Escherichia coli PTS, the panC transgene increases the total PTS activity in leaves of trangenic plants by up to 500fold but does not affect the steady-state level of pantothenate, overviewEscherichia coli-694696
overexpression as a fusion protein with cytochrome b5 in Escherichia coli BL21(DE3). The advantages of the cytochrome b5 fusion system are its high expression levels in both rich and minimal medium, high solubility, stability, ease of purification, small size, and characteristic colorEscherichia coli-663315
expression in Escherichia coliFusarium oxysporumQ96VJ9653240
expression Escherichia coliLotus japonicusO24035649671
expression in Escherichia coliMycobacterium tuberculosis-650029, 650212, 653802
wild-type and mutant enzymes expressed in Escherichia coli BL21Mycobacterium tuberculosis-661144
-Oryza sativaO24210649671
expressed in Escherichia coli as a His-tagged fusion proteinStaphylococcus aureusQ2FV22714204

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

ENGINEERINGORGANISM UNIPROT ACCESSION NO.COMMENTARYLITERATURE
D63GEscherichia coli-mutation increases the mobility of the gate loop in Escherichia coli pantothenate synthetase716880
E77GMycobacterium tuberculosis-87% of wild-type activity653802
G74DMycobacterium tuberculosis-mutation reduces the mobility of the gate loop in Mycobacterium tuberculosis pantothenate synthetase716880
H44AMycobacterium tuberculosis-greater than 1000fold reduction in enzyme activity661144
H47AMycobacterium tuberculosis-greater than 1000fold reduction in enzyme activity661144
K160AMycobacterium tuberculosis-greater than 1000fold reduction in enzyme activity661144
K160CMycobacterium tuberculosis-activity is markedly enhanced by the alkylation of cysteine with bromoethylamine661144
N69AMycobacterium tuberculosis-greater than 1000fold reduction in enzyme activity661144
Q164AMycobacterium tuberculosis-mutant exhibits 50fold less activity than wild-type enzyme661144
Q72AMycobacterium tuberculosis-greater than 1000fold reduction in enzyme activity661144
E132AArabidopsis thaliana-kcat for beta-alanine is 3.7fold higher than wild-type value, kcat for pantoate is 21fold higher than wild-type value674714
additional informationArabidopsis thalianaQ9FKB3construction of an uxotrophic AtPTS knockout mutant, phenotype, overview. Complementation of the mutant phenotype by heterologous expression of Escherichia coli PTS gene panC. The panC transgene increases the total PTS activity in leaves by up to 500fold but does not affect the steady-state level of pantothenate. The AtPTS knockout phenotype is rescued by exogenous pantothenate694696

Renatured/COMMENTARYORGANISM UNIPROT ACCESSION NO.LITERATURE
No entries in this field

APPLICATIONORGANISM UNIPROT ACCESSION NO.COMMENTARYLITERATURE
No entries in this field

REF. AUTHORS TITLE JOURNAL VOL. PAGES YEAR ORGANISMLINK TO PUBMEDSOURCE
975Cronan, J.E.; Littel, K.J.; Jackowski, S.Genetic and biochemical analyses of pantothenate biosynthesis in Escherichia coli and Salmonella typhimuriumJ. Bacteriol.149916-9221982Escherichia coli, Salmonella enterica subsp. enterica serovar Typhimurium PubMed
976Cronan, J.E.Enzymatic synthesis of beta-[U-14C]alanine and D-[1,2,3-14C]pantothenate of high specific radioactivityAnal. Biochem.103377-3801980Escherichia coli PubMed
977Miyatake, K.; Nakano, Y.; Kitaoka, S.Pantothenate synthetase from Escherichia coli [D-pantoate:beta-alanine ligase (AMP-forming), EC 6.3.2.1]Methods Enzymol.62215-2191979Escherichia coli PubMed
978Miyatake, K.; Nakano, Y.; Kitaoka, S.Enzymological properties of pantothenate synthetase from Escherichia coli BJ. Nutr. Sci. Vitaminol.24243-2531978Escherichia coli PubMed
979Miyatake, K.; Nakano, Y.; Kitaoka, S.Some properties of pantothenate synthetase partially purified from Escherichia coli BBull. Univ. Osaka Prefect2757-671975Escherichia coli-
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LINKS TO OTHER DATABASES (specific for EC-Number 6.3.2.1)
ExplorEnz
ExPASy
KEGG
MetaCyc
NCBI: PubMed, Protein, Nucleotide, Structure, Genome, OMIM
IUBMB Enzyme Nomenclature
PROSITE Database of protein families and domains
SYSTERS
Protein Mutant Database
InterPro (database of protein families, domains and functional sites)