Information on EC 6.3.2.8 - UDP-N-acetylmuramate-L-alanine ligase

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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
6.3.2.8
-
RECOMMENDED NAME
GeneOntology No.
UDP-N-acetylmuramate-L-alanine ligase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
ATP + UDP-N-acetyl-alpha-D-muramate + L-alanine = ADP + phosphate + UDP-N-acetyl-alpha-D-muramoyl-L-alanine
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
carboxamide formation
-
-
-
-
carboxylic acid amide formation
-
-
-
-
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
D-Glutamine and D-glutamate metabolism
-
-
Metabolic pathways
-
-
Peptidoglycan biosynthesis
-
-
UDP-N-acetylmuramoyl-pentapeptide biosynthesis I (meso-diaminopimelate containing)
-
-
UDP-N-acetylmuramoyl-pentapeptide biosynthesis II (lysine-containing)
-
-
peptidoglycan biosynthesis
-
-
SYSTEMATIC NAME
IUBMB Comments
UDP-N-acetylmuramate:L-alanine ligase (ADP-forming)
Involved in the synthesis of a cell-wall peptide in bacteria.
CAS REGISTRY NUMBER
COMMENTARY hide
9023-52-3
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
strain L2
-
-
Manually annotated by BRENDA team
strain L2
-
-
Manually annotated by BRENDA team
gene murC
-
-
Manually annotated by BRENDA team
strain JM83(pAM1005)
-
-
Manually annotated by BRENDA team
K12HfrH
-
-
Manually annotated by BRENDA team
9602
-
-
Manually annotated by BRENDA team
strain CPAO1
-
-
Manually annotated by BRENDA team
strain CPAO1
-
-
Manually annotated by BRENDA team
strain Copenhagen
-
-
Manually annotated by BRENDA team
strain MSB8
SwissProt
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
additional information
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
ATP + dihydro-UDP-N-acetylmuramate + L-Ala
ADP + phosphate + dihydro-UDP-N-acetylmuramoyl-L-Ala
show the reaction diagram
-
-
-
-
-
ATP + UDP-N-acetylglucosaminyl-enoylpyruvate + L-Ala
ADP + phosphate + UDP-N-acetylglucosaminyl-enoylpyruvoyl-L-Ala
show the reaction diagram
-
-
-
-
-
ATP + UDP-N-acetylmuramate + 2-amino-N-butyric acid
ADP + phosphate + UDP-N-acetylmuramoyl-2-amino-N-butyric acid
show the reaction diagram
ATP + UDP-N-acetylmuramate + 2-amino-N-hydroxymethyl propionamide
ADP + phosphate + UDP-N-acetylmuramoyl-2-amino-N-hydroxymethylpropionamide
show the reaction diagram
-
-
-
-
-
ATP + UDP-N-acetylmuramate + 2-amino-propionamide
ADP + phosphate + UDP-N-acetylmuramoyl-2-aminopropionamide
show the reaction diagram
-
-
-
-
-
ATP + UDP-N-acetylmuramate + 2-amino-tert-butylpropionate
ADP + phosphate + UDP-N-acetylmuramoyl-2-amino-tert-butylpropionate
show the reaction diagram
-
-
-
-
-
ATP + UDP-N-acetylmuramate + benzyl L-alaninate
ADP + phosphate + benzyl UDP-N-acetylmuramoyl-L-alanine
show the reaction diagram
-
-
-
-
-
ATP + UDP-N-acetylmuramate + beta-Ala
ADP + phosphate + UDP-N-acetylmuramoyl-beta-Ala
show the reaction diagram
-
-
-
-
-
ATP + UDP-N-acetylmuramate + beta-chloro-L-Ala
ADP + phosphate + UDP-N-acetylmuramoyl-beta-chloro-L-Ala
show the reaction diagram
-
-
-
-
-
ATP + UDP-N-acetylmuramate + beta-cyano-L-Ala
ADP + phosphate + UDP-N-acetylmuramoyl-beta-cyano-L-Ala
show the reaction diagram
-
-
-
-
-
ATP + UDP-N-acetylmuramate + DL-propargylglycine
ADP + phosphate + UDP-N-acetylmuramoyl-DL-propargylglycine
show the reaction diagram
-
-
-
-
-
ATP + UDP-N-acetylmuramate + DL-Ser
ADP + phosphate + UDP-N-acetylmuramoyl-DL-Ser
show the reaction diagram
ATP + UDP-N-acetylmuramate + ethyl L-alaninate
ADP + phosphate + ethyl UDP-N-acetylmuramoyl-L-alaninate
show the reaction diagram
-
-
-
-
-
ATP + UDP-N-acetylmuramate + Gly
ADP + phosphate + UDP-N-acetylmuramoyl-Gly
show the reaction diagram
ATP + UDP-N-acetylmuramate + glycine
ADP + phosphate + UDP-N-acetylmuramoyl-glycine
show the reaction diagram
ATP + UDP-N-acetylmuramate + L-Ala
?
show the reaction diagram
ATP + UDP-N-acetylmuramate + L-Ala
ADP + phosphate + UDP-N-acetylmuramoyl-L-Ala
show the reaction diagram
ATP + UDP-N-acetylmuramate + L-alanine
ADP + phosphate + UDP-N-acetylmuramoyl-L-alanine
show the reaction diagram
ATP + UDP-N-acetylmuramate + L-Cys
ADP + phosphate + UDP-N-acetylmuramoyl-L-Cys
show the reaction diagram
-
-
-
-
-
ATP + UDP-N-acetylmuramate + L-Ile
ADP + phosphate + UDP-N-acetylmuramoyl-L-Ile
show the reaction diagram
-
-
-
-
-
ATP + UDP-N-acetylmuramate + L-serine
ADP + phosphate + UDP-N-acetylmuramoyl-L-serine
show the reaction diagram
ATP + UDP-N-acetylmuramate + L-Thr
ADP + phosphate + UDP-N-acetylmuramoyl-L-Thr
show the reaction diagram
-
-
-
-
-
ATP + UDP-N-acetylmuramate + L-Val
ADP + phosphate + UDP-N-acetylmuramoyl-L-Val
show the reaction diagram
-
-
-
-
-
ATP + UDP-N-acetylmuramate + L-vinylglycine
ADP + phosphate + UDP-N-acetylmuramoyl-L-vinylglycine
show the reaction diagram
-
-
-
-
-
ATP + UDP-N-acetylmuramate + methyl L-alaninate
ADP + phosphate + methyl UDP-N-acetylmuramoyl-L-alaninate
show the reaction diagram
-
-
-
-
-
ATP + UDP-N-acetylmuramate + N-(2-aminopropionyl)piperidine
ADP + phosphate + UDP-N-acetylmuramoyl-N-(2-aminopropionyl)piperidine
show the reaction diagram
-
-
-
-
-
UTP + UDP-N-acetylmuramate + L-Ala
UDP + phosphate + UDP-N-acetylmuramoyl-L-Ala
show the reaction diagram
-
about 11% of the activity relative to ATP
-
-
additional information
?
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
ATP + UDP-N-acetylmuramate + L-Ala
?
show the reaction diagram
ATP + UDP-N-acetylmuramate + L-alanine
ADP + phosphate + UDP-N-acetylmuramoyl-L-alanine
show the reaction diagram
additional information
?
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
(NH4)2SO4
-
stimulation by 5-25 mM
K+
-
monovalent cation required, NH4+ or K+
MgCl2
-
dependent with maximal enzymatic activity at 20mM MgCl2
NH4+
-
monovalent cation required, NH4+ or K+
Zn2+
-
can partially substitute for Mg2+
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
(5Z)-5-([2-[(4-chlorobenzyl)sulfanyl]-5-nitrophenyl]methylidene)-2-thioxo-1,3-thiazolidin-4-one
-
-
(5Z)-5-([4-[(E)-2-phenylethenyl]phenyl]methylidene)-2-thioxo-1,3-thiazolidin-4-one
-
-
1H-indazole-3-carbohydrazide
-
-
2-((4-[(2S)-butan-2-ylamino]-6-(ethylamino)-1,3,5-triazin-2-yl)sulfanyl)-N-(2-chlorophenyl)acetamide
-
0.5 mM, 26% inhibition
2-(4-{[(E)-2-(1H-indazol-3-ylcarbonyl)hydrazono]methyl} phenoxy) acetic acid
-
complete inhibition at 0.5 mM
2-([2-(2-naphthylsulfonyl)hydrazono)methyl]phenyl 2-nitrobenzenesulfonate
-
55% inhibition at 0.05 mM
2-([2-(2-naphthylsulfonyl)hydrazono)methyl]phenyl 3-nitrobenzenesulfonate
-
65% inhibition at 0.05 mM
2-([2-(2-naphthylsulfonyl)hydrazono)methyl]phenyl 4-nitrobenzenesulfonate
-
75% inhibition at 0.10 mM
2-([2-(naphthalen-2-ylsulfonyl)hydrazono]methyl)phenyl 2-(benzo[d][1,3]dioxol-5-yl)acetate
-
57% inhibition at 0.10 mM
2-bromo-N-(4-([2-(2-naphthylsulfonyl)hydrazono]methyl)phenyl)benzamide
-
41% inhibition at 0.10 mM
2-phenyl-1,3-thiazole-5-carbohydrazide
-
-
2-phenyl-N'-[(E)-(2,3,4-trihydroxyphenyl)methylidene]-1,3-thiazole-5-carbohydrazide
-
18% inhibition at 0.25 mM
2-[4-({(E)-2-[(4-methyl-1,3-thiazol-5-yl)carbonyl]hydrazono} methyl)phenoxy]acetic acid
-
complete inhibition at 0.5 mM
3,3,3-Trifluoro-DL-Ala
-
-
3,3-Difluoro-L-Ala
-
-
3-bromo-N-(4-([2-(2-naphthylsulfonyl)hydrazono]methyl)phenyl)benzamide
-
-
3-Fluoro-L-Ala
-
-
4-([(5-methyl-1,3,4-thiadiazol-2-yl)sulfanyl]methyl)-6-(naphthalen-2-ylmethyl)-1,3,5-triazin-2-amine
-
0.5 mM, 30% inhibition
4-({(E)-2-[(4-methyl-1,3-thiazol-5-yl)carbonyl]hydrazono} methyl)benzoic acid
-
94% inhibition at 0.5 mM
4-cyano-N-(4-([2-(2-naphthylsulfonyl)hydrazono]methyl)phenyl)benzamide
-
91% inhibition at 0.05 mM
4-methyl-1,3-thiazole-5-carbohydrazide
-
-
4-methyl-N'-[(E)-(2,3,4-trihydroxyphenyl)methylidene]-1,3-thiazole-5-carbohydrazide
-
26% inhibition at 0.5 mM
4-methyl-N'-[(E)-(2-phenyl-1,3-thiazol-4-yl)methylidene]-1,3-thiazole-5-carbohydrazide
-
complete inhibition at 0.5 mM
4-{[(E)-2-(1H-indazol-3-ylcarbonyl)hydrazono]methyl}benzoic acid
-
complete inhibition at 0.5 mM
5-methyl-N-([4-(5-phenyl-1-benzofuran-2-yl)phenyl]sulfonyl)thiophene-2-carboxamide
-
IC50 2.3 microM
6-([(1,1-dioxidotetrahydrothiophen-3-yl)sulfanyl]methyl)-N-(2-phenylethyl)-1,3,5-triazine-2,4-diamine
-
0.25 mM, 32% inhibition
6-[(1-methyl-1H-imidazol-2-yl)sulfanyl]-N,N'-diphenyl-1,3,5-triazine-2,4-diamine
-
0.5 mM, 36% inhibition
Ba2+
-
inhibits activation by Mn2+
benzohydrazide
-
-
benzylidene rhodanines
-
possess MurC inhibitory activity in the low micromolar range
-
beta-gamma-methyleneadenosine 5'-triphosphate
-
-
Cd2+
-
inhibits activation by Mn2+
Co2+
-
inhibits activation by Mn2+
Fe2+
-
inhibits activation by Mn2+
feglymycin
Hg2+
-
inhibits activation by Mn2+
KCl
-
inhibition above 100 mM
L-2-aminobutyrate
-
-
L-Ala-L-1-aminoethylphosphinic acid
-
i.e. alaphosphin
L-Allylglycine
-
weak
L-Cys
-
weak
L-lactate
-
-
L-Propargylglycine
-
-
L-Ser
L-Vinylglycine
-
-
methyl4-({(E)-2-[(4-methyl-1,3-thiazol-5-yl)carbonyl]hydrazono}methyl)benzoate
-
95% inhibition at 0.5 mM
methyl4-{[(E)-2-(1H-indazol-3-ylcarbonyl)hydrazono]methyl} benzoate
-
complete inhibition at 0.5 mM
Mg2+
-
inhibits activation by Mn2+
N'-((2-[(2-nitrobenzyl)oxy]phenyl)methylidene)-2-naphthalenesulfonohydrazide
-
30% inhibition at 0.10 mM
N'-((2-[(3-nitrobenzyl)oxy]phenyl)methylidene)-2-naphthalenesulfonohydrazide
-
36% inhibition at 0.05 mM
N'-((2-[(4-cyanobenzyl)oxy]phenyl)methylidene)(2-fluorophenyl)methanesulfonohydrazide
-
59% inhibition at 0.10 mM
N'-((2-[(4-cyanobenzyl)oxy]phenyl)methylidene)(phenyl)methanesulfonohydrazide
-
complete inhibition at 0.10 mM
N'-((2-[(4-cyanobenzyl)oxy]phenyl)methylidene)-2-naphthalenesulfonohydrazide
-
36% inhibition at 0.10 mM
N'-((2-[(4-cyanobenzyl)oxy]phenyl)methylidene)-2-nitrobenzenesulfonohydrazide
-
95% inhibition at 0.01 mM
N'-((2-[(4-cyanobenzyl)oxy]phenyl)methylidene)-3-nitrobenzenesulfonohydrazide
-
-
N'-((2-[(4-cyanobenzyl)oxy]phenyl)methylidene)[4-(trifluoromethyl)phenyl]methanesulfonohydrazide
-
-
N'-((3-[(3-nitrobenzyl)oxy]phenyl)methylidene)-2-naphthalenesulfonohydrazide
-
58% inhibition at 0.05 mM
N'-[(E)-(2,3,4-trihydroxyphenyl)methylidene]-1H-indazole-3-carbohydrazide
-
42% inhibition at 0.25 mM
N'-[(E)-(2,3,4-trihydroxyphenyl)methylidene]benzohydrazide
-
64% inhibition at 0.10 mM
N'-[(E)-(2,4-dihydroxyphenyl)methylidene]-1H-indazole-3-carbohydrazide
-
74% inhibition at 0.25 mM
N'-[(E)-(2-hydroxyphenyl)methylidene]-1H-indazole-3-carbohydrazide
-
complete inhibition at 0.25 mM
N'-[(E)-(2-phenyl-1,3-thiazol-4-yl)methylidene]-1H-indazole-3-carbohydrazide
-
78% inhibition at 0.10 mM
N'-[(E)-(2-phenyl-1,3-thiazol-4-yl)methylidene]benzohydrazide
-
70% inhibition at 0.25 mM
N'-[(E)-(3,4-dihydroxyphenyl)methylidene]-1H-indazole-3-carbohydrazide
-
36% inhibition at 0.5 mM
N'-[(E)-(3,4-dihydroxyphenyl)methylidene]-4-methyl-1,3-thiazole-5-carbohydrazide
-
95% inhibition at 0.5 mM
N'-[(E)-(3,4-dihydroxyphenyl)methylidene]benzohydrazide
-
complete inhibition at 0.5 mM
N'-[(E)-(3,4-dimethoxyphenyl)methylidene]-1H-indazole-3-carbohydrazide
-
complete inhibition at 0.5 mM
N'-[(E)-(3,4-dimethoxyphenyl)methylidene]-4-methyl-1,3-thiazole-5-carbohydrazide
-
complete inhibition at 0.5 mM
N'-[(E)-(3,4-dimethoxyphenyl)methylidene]benzohydrazide
-
97% inhibition at 0.5 mM
N'-[(E)-(3,5-dichloro-2-hydroxyphenyl)methylidene]-4-methyl-1,3-thiazole-5-carbohydrazide
-
43% inhibition at 0.25 mM
N'-[(E)-(3-hydroxy-4-methoxyphenyl)methylidene] benzohydrazide
-
92% inhibition at 0.5 mM
N'-[(E)-(3-hydroxy-4-methoxyphenyl)methylidene]-1H-indazole-3-carbohydrazide
-
67% inhibition at 0.25 mM
N'-[(E)-(4-cyanophenyl)methylidene]-1H-indazole-3-carbohydrazide
-
complete inhibition at 0.25 mM
N'-[(E)-(4-cyanophenyl)methylidene]benzohydrazide
-
complete inhibition at 0.25 mM
N'-[(E)-(4-nitrophenyl)methylidene]-1H-indazole-3-carbohydrazide
-
91% inhibition at 0.5 mM
N'-[(E)-1H-indol-3-ylmethylidene]-1H-indazole-3-carbohydrazide
-
complete inhibition at 010 mM
N'-[(E)-1H-indol-3-ylmethylidene]benzohydrazide
-
93% inhibition at 0.5 mM
N'-{(E)-[4-(dimethylamino)phenyl]methylidene}-1H-indazole-3-carbohydrazide
-
95% inhibition at 0.25 mM
N'-{(E)-[4-(dimethylamino)phenyl]methylidene}-4-methyl-1,3-thiazole-5-carbohydrazide
-
97% inhibition at 0.25 mM
N'-{(E)-[4-(dimethylamino)phenyl]methylidene}benzohydrazide
-
complete inhibition at 0.25 mM
N-(2-([2-(2-naphthylsulfonyl)hydrazono]methyl)phenyl)-3,5-dinitrobenzamide
-
51% inhibition at 0.10 mM
N-(2-([2-(2-naphthylsulfonyl)hydrazono]methyl)phenyl)-4-nitrobenzamide
-
-
N-(4-([2-(2-naphthylsulfonyl)hydrazono]methyl)phenyl)-2-naphthamide
-
-
N-(4-([2-(2-naphthylsulfonyl)hydrazono]methyl)phenyl)-2-nitrobenzamide
-
-
N-(4-([2-(2-naphthylsulfonyl)hydrazono]methyl)phenyl)-3,5-dinitrobenzamide
-
72% inhibition at 0.10 mM
N-(4-([2-(2-naphthylsulfonyl)hydrazono]methyl)phenyl)-4-nitrobenzamide
-
71% inhibition at 0.05 mM
N-(4-([2-(2-naphthylsulfonyl)hydrazono]methyl)phenyl)benzamide
-
97% inhibition at 0.10 mM
N-Methyl-L-Ala
-
weak
N-[(E)-(2,4-dihydroxyphenyl)methylidene]benzohydrazide
-
complete inhibition at 0.5 mM
NaCl
-
inhibition above 100 mM
p-hydroxymercuribenzoate
-
partial protection by ATP
potassium phosphate
-
no effect up to 20 mM, significant decrease of activity at higher concentrations
UDP-2-(acetylamino)-4-O-[[(2-carboxypropyl)(hydroxy)phosphoryl]methyl]-2-deoxy-alpha-D-glucopyranose
-
-
UDP-N-acetylmuramoyl-L-Ala
-
-
additional information
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2-mercaptoethanol
ammonium sulfate
-
20% stimulation at concentrations above 25mM
Cys
-
stimulates
dithiothreitol
-
stimulates
glutathione
-
stimulates
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
4.3
2-amino-n-butyric acid
-
-
16
2-amino-N-hydroxymethyl propionamide
-
-
7.9
2-aminopropionamide
-
-
0.0638 - 2
ATP
0.36
benzyl L-alaninate
-
-
0.046
beta-Ala
-
-
2
beta-anomer UDP-N-acetylmuramate
-
-
0.173
beta-chloro-L-Ala
-
-
0.19
beta-cyano-L-Ala
-
-
1
dihydro-UDP-N-acetylmuramate
-
-
1.1
DL-propargylglycine
-
-
0.59
ethyl L-alaninate
-
-
2.5 - 29
Gly
0.0258 - 1.17
glycine
0.02 - 0.44
L-Ala
0.01 - 0.3
L-alanine
3.8
L-Cys
-
-
40
L-Ile
-
-
1.2 - 1.99
L-Ser
0.0997 - 0.242
L-serine
25
L-Thr
-
-
70
L-Val
-
-
0.44
L-Vinylglycine
-
-
0.5
methyl L-alaninate
-
-
62
N-(2-aminopropionyl)piperidine
-
-
0.22
N-acetylmuramate
-
-
0.85
Ser
-
-
0.43
UDP-N-acetylglucosyl-enolpyruvate
-
-
0.01 - 1.1
UDP-N-acetylmuramate
additional information
additional information
-
Km-value of wild-type and mutant enzymes
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
13.5
2-amino-benzylpropionate
Escherichia coli
-
-
15.2
2-amino-ethylpropionate
Escherichia coli
-
-
28.3
2-amino-methylpropionate
Escherichia coli
-
-
25
2-amino-n-butyric acid
Escherichia coli
-
-
11.7
2-amino-N-hydroxymethylpropionamide
Escherichia coli
-
-
18.3
2-amino-propionamide
Escherichia coli
-
-
21.7
2-amino-tert-butylpropionate
Escherichia coli
-
-
2.5
beta-Alanine
Escherichia coli
-
-
20
beta-chloro-Ala
Escherichia coli
-
-
11.1
beta-chloro-L-Ala
Escherichia coli
-
-
26.7
beta-cyano-L-Ala
Escherichia coli
-
-
20
DL-propargylglycine
Escherichia coli
-
-
11.7 - 21.7
Gly
1.53
glycine
Mycobacterium tuberculosis
-
pH 8.5, 37°C, recombinant enzyme
6.85 - 16.3
L-Ala
1
L-alanine
Mycobacterium tuberculosis
-
pH 8.5, 37°C, recombinant enzyme
20
L-Cys
Escherichia coli
-
-
5.17
L-Ile
Escherichia coli
-
-
11.4 - 25
L-Ser
1.2
L-serine
Mycobacterium tuberculosis
-
pH 8.5, 37°C, recombinant enzyme
23.3
L-Thr
Escherichia coli
-
-
21.7
L-Val
Escherichia coli
-
-
15.3
L-Vinylglycine
Escherichia coli
-
-
6.17
N-(2-aminopropionyl)piperidine
Escherichia coli
-
-
additional information
additional information
-
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
15.1
ATP
Mycobacterium tuberculosis
-
pH 8.5, 37°C, recombinant enzyme
4
10.47
glycine
Mycobacterium tuberculosis
-
pH 8.5, 37°C, recombinant enzyme
72
23.9
L-alanine
Mycobacterium tuberculosis
-
pH 8.5, 37°C, recombinant enzyme
103
12.5
L-serine
Mycobacterium tuberculosis
-
pH 8.5, 37°C, recombinant enzyme
95
44.8
UDP-N-acetylmuramate
Mycobacterium tuberculosis
-
pH 8.5, 37°C, recombinant enzyme
1940
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0045 - 0.0063
5-methyl-N-([4-(5-phenyl-1-benzofuran-2-yl)phenyl]sulfonyl)thiophene-2-carboxamide
0.0003 - 0.001
feglymycin
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.027
(5Z)-5-([2-[(4-chlorobenzyl)sulfanyl]-5-nitrophenyl]methylidene)-2-thioxo-1,3-thiazolidin-4-one
Escherichia coli
-
pH 8.0, 37°C
0.018
(5Z)-5-([4-[(E)-2-phenylethenyl]phenyl]methylidene)-2-thioxo-1,3-thiazolidin-4-one
Escherichia coli
-
pH 8.0, 37°C
0.123
1H-indazole-3-carbohydrazide
Escherichia coli
-
pH 8.0, 37°C
0.032
2-phenyl-N'-[(E)-(2,3,4-trihydroxyphenyl)methylidene]-1,3-thiazole-5-carbohydrazide
Escherichia coli
-
pH 8.0, 37°C
0.03
3-bromo-N-(4-([2-(2-naphthylsulfonyl)hydrazono]methyl)phenyl)benzamide
Escherichia coli
-
pH 8.0, 37°C
0.0023
5-methyl-N-([4-(5-phenyl-1-benzofuran-2-yl)phenyl]sulfonyl)thiophene-2-carboxamide
Escherichia coli
-
Compound A, IC50 2.3 microM
0.027
N-(2-([2-(2-naphthylsulfonyl)hydrazono]methyl)phenyl)-4-nitrobenzamide
Escherichia coli
-
pH 8.0, 37°C
0.031
N-(4-([2-(2-naphthylsulfonyl)hydrazono]methyl)phenyl)-2-naphthamide
Escherichia coli
-
pH 8.0, 37°C
0.051
N-(4-([2-(2-naphthylsulfonyl)hydrazono]methyl)phenyl)-2-nitrobenzamide
Escherichia coli
-
pH 8.0, 37°C
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.074
-
37°C, pH 8.6
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.5 - 8.5
-
-
7.8 - 8.5
-
-
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5.5 - 10.5
-
-
7.5 - 10
-
7.5: about 70% of maximal activity, 10.0: about 95% of maximal activity
7.5 - 9
-
pH 7.5: about 60% of maximal activity, pH 9.0: about 70% of maximal activity
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
-
50% decay of activity after the end of exponential cell division
Manually annotated by BRENDA team
PDB
SCOP
CATH
ORGANISM
UNIPROT
Escherichia coli (strain K12)
Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd)
Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd)
Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd)
Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd)
Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
40000
-
gel filtration in absence and in presence of 2.5 mM 2-mercaptoethanol
50000
-
x * 50000, SDS-PAGE
51740
calculated
52000
-
x * 52000, recombinant detagged enzyme, SDS-PAGE
53630
-
mass spectrometry
53640
-
mass spectrometry
53750
-
trifluoroacetic adduct by mass spectrometry
53880
-
trifluoroacetic adduct by mass spectrometry
53990
-
trifluoroacetic adduct by mass spectrometry
54000
2 * 54000 by crystallographic analysis
54486
-
1 * 54486, calculation from nucleotide sequence, electrospray ionization mass spectrometry, enzyme exists in equilibrium between monomeric and dimeric form, sedimentation equilibrium analysis at multiple speeds and multiple concentrations; 2 * 54486, calculation from nucleotide sequence, electrospray mass spectrometry, enzyme exists in equilibrium between monomeric and dimeric form, sedimentation equilibrium analysis at multiple speeds and multiple concentrations
57760
-
calculated for the His- and S-tagged enzyme; mass spectrometry of the recombinant enzyme
65000
-
gel filtration of the recombinant enzyme
100000
dynamic light-scattering analysis
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
monomer
-
1 * 54486, calculation from nucleotide sequence, electrospray ionization mass spectrometry, enzyme exists in equilibrium between monomeric and dimeric form, sedimentation equilibrium analysis at multiple speeds and multiple concentrations
additional information
MurC domain structure and three-dimensional structure modeling by homology modeling method, structure comparisons of Mur ligases, overview
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
phosphoprotein
-
MurC is phosphorylated in vitro by the PknA protein kinase, but not by PknG kinase, exclusively on threonine residues, which has regulatory function, mutation of the phosphorylation site threonine residues impairs enzyme activity, double phosphorylation of the activation loop residues Thr179 and Thr181 is necessary for full kinase activity
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
crystal structure of Escherichia coli UDP-N-acetylmuramoyl:L-alanine ligase determined to 2.6 A resolution. The structure is solved by multiwavelength anomalous diffraction methods from a single selenomethionine-substituted crystal and refined to a crystallographic R factor of 0.212. Crystals of both native and SeMet-substituted EcMurC belong to space group P2(1)2(1)2(1), with unit-cell parameters a = 73.9 A, b = 93.6 A, c = 176.8 A. The SeMet crystals give the best quality diffraction data
-
crystals obtained in both native and selenemethionine forms
crystal structure of active fully assembled substrate- and product-bound complexes. Selenomethionine-substituted enzyme preparations used for structure determination. Crystals obtained by drop vapor diffusion experiments
construction of 3-D structure using templates PDB codes 1GQQ and 1P31. Residues G125, K126, R331, and R332 within the binding pocket are important in ligand and substrate binding affinity and selectivity
-
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.2
-
5 mM potassium phosphate, 50°C, 20 min, 10-20% loss of activity. 60-90% loss of activity in 250 mM potassium phosphate buffer
1280
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
10 - 70
-
purified recombinant His-tagged enzyme, stable up to 40°C, MurC activity diminishes at 45-70°C
37
-
28% loss of activity with previous remove of dithiothreitol
50
-
5 mM potassium phosphate, pH 7.2, 20 min, 10-20% loss of activity. 60-90% loss of activity in 250 mM potassium phosphate buffer
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
decrease in stability at high salt concentrations is prevented by addition of 10% glycerol and 2.5 mM 2-mercaptoethanol
-
presence of 2-mercaptoethanol and glycerol is essential for stability
-
relatively stable at low ionic strength, unstable at high concentrations of salt
-
stability is strictly dependent on the presence of 2-mercaptoethanol
-
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-18°C, 5 mM potassium phosphate, 10-20% loss of activity after 3 months
-
-20°C, 20 mM potassium phosphate, pH 7.2, 1 mM EDTA, 2.5 mM 2-mercaptoethanol, 15% glycerol
-
25°C, purified recombinant His-tagged enzyme, 50% loss of activity, 1 week
-
4°C, 5 mM potassium phosphate, overnight, 10-20% loss of activity. At 4°C, 250 mM potassium phosphate, 12 h, 30% loss of activity
-
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
method that includes chromatography using a Ni-nitrilotriacetic acid Superflow agarose-filled column and gel filtration
-
partial
purified with ProBond nickel-chelating resin
recombinant His-tagged wild-type and mutant enzymes from Escherichia coli strain BL21(DE3), the His-tag is cleaved off by TEV protease
-
recombinant MurC from Escherichia coli strain JM83 by anion exchange chromatography
-
recombinant protein
-
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli
expressed in Escherichia coli BL21(DE3)
expressed in Escherichia coli JM83 and PC2453
-
expressed in Escherichia coli strain BL21
-
expression in Escherichia coli
-
expression of TM0231 in Escherichia coli DL41
functionally expressed in Escherichia coli H1119, temperature-sensitive, using the pET30a vector
-
gene murC, expression of N-terminally His-tagged wild-type and mutant enzymes as soluble proteins in Escherichia coli strain BL21(DE3), cloning in Corynebacterium glutamicum strain ATCC 13869
-
gene murC, located in the division/cell wall (dcw) cluster, identification of a promoter driving the co-transcription of mur synthetases along with key cell division genes such as ftsQ and ftsW, recombinant expression of His6-tagged enzyme in Escherichia coli BL21(DE3)/pLysS and Pseudomonas putida KT2442, subcloning in Escherichia coli strain DH5alpha. Coexpression of genes murC/D/E/F/nat and genes pknA, pknB, murI, dapF, ddlA, namH, Rv2160c, ftsW, ftsQ, ftsZ, sepF, wag31 in Mycobacterium smegmatis
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murC gene is amplified by PCR and cloned with the expression vector pTrc99A
-
MurC, overexpression in Escherichia coli strain JM83
-
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
T362A/T365A/T51A
-
site-directed mutagenesis, the mutant shows impaired activity
T362A/T365A/T51A/T120A
-
site-directed mutagenesis, the mutant shows impaired activity
T362A/T365A/T51A/T120A/T167A
-
site-directed mutagenesis, the mutant shows impaired activity
T362A/T365A/T51A/T120A/T167A/T133A
-
site-directed mutagenesis, the mutant shows impaired activity
C230A
-
activity completely lost at 42°C
C426A
-
Km increased 3fold for ATP and 10fold for UDP-MurNAc and L-alanine, with respect to the wild-type
H199A
-
mutant enzymes K130A, H199A, N293A, N296A, and R327A lead to important variations of the Km value for one or more substrates
K130A
-
mutant enzymes K130A, H199A, N293A, N296A, and R327A lead to important variations of the Km value for one or more substrates
N293A
-
mutant enzymes K130A, H199A, N293A, N296A, and R327A lead to important variations of the Km value for one or more substrates
N296A
-
mutant enzymes K130A, H199A, N293A, N296A, and R327A lead to important variations of the Km value for one or more substrates
R327A
-
mutant enzymes K130A, H199A, N293A, N296A, and R327A lead to important variations of the Km value for one or more substrates
TOF-123
-
mutant enzyme TOF-95 is almost indistinguishable from wild type, mutant enzymes TOF-9 and TOF-123 have alanine-adding activity about 60% of the wild type at both 30 C and 43 C
TOF-9
-
mutant enzyme TOF-95 is almost indistinguishable from wild type, mutant enzymes TOF-9 and TOF-123 have alanine-adding activity about 60% of the wild type at both 30 C and 43 C
TOF-95
-
mutant enzyme TOF-95 is almost indistinguishable from wild type, mutant enzymes TOF-9 and TOF-123 have alanine-adding activity about 60% of the wild type at both 30 C and 43 C
additional information
-
mutation of the phosphorylation site threonine residues highly impairs enzyme activity
Show AA Sequence (13306 entries)
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