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Information on EC 2.5.1.7 - UDP-N-acetylglucosamine 1-carboxyvinyltransferase and Organism(s) Pseudomonas aeruginosa

for references in articles please use BRENDA:EC2.5.1.7

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The taxonomic range for the selected organisms is: Pseudomonas aeruginosa
The expected taxonomic range for this enzyme is: Bacteria, Archaea, Eukaryota

Synonyms
udp-n-acetylglucosamine enolpyruvyl transferase, mura enzyme, muraa, udp-n-acetylglucosamine 1-carboxyvinyltransferase, udp-n-acetylglucosamine enolpyruvyltransferase, udp-nag enolpyruvyl transferase, udp-n-acetylglucosamine 1-carboxyvinyl-transferase, udp-glcnac enolpyruvyl transferase, udp-n-acetylglucosamine 1-carboxyvinyl transferase, udp-n-acetylglucosamine enolpyruvyle transferase, more

SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
enoylpyruvate transferase
-
-
-
-
enoylpyruvatetransferase
-
-
-
-
MurA enzyme
-
-
MurA transferase
-
-
-
-
phosphoenolpyruvate-UDP-acetylglucosamine-3-enolpyruvyltransferase
-
-
-
-
phosphoenolpyruvate:UDP-2-acetamido-2-deoxy-D-glucose 2-enoyl-1-carboxyethyltransferase
-
-
-
-
phosphoenolpyruvate:uridine diphosphate N-acetylglucosamine enolpyruvyltransferase
-
-
-
-
phosphoenolpyruvate:uridine-5'-diphospho-N-acetyl-2-amino-2-deoxyglucose-3-enolpyruvyltransferase
-
-
-
-
phosphopyruvate-uridine diphosphoacetylglucosamine pyruvatetransferase
-
-
-
-
pyruvate-UDP-acetylglucosamine transferase
-
-
-
-
pyruvate-uridine diphospho-N-acetyl-glucosamine transferase
-
-
-
-
pyruvate-uridine diphospho-N-acetylglucosamine transferase
-
-
-
-
pyruvatetransferase, phosphoenolpyruvate-uridine diphosphoacetylglucosamine
-
-
-
-
pyruvic-uridine diphospho-N-acetylglucosaminyltransferase
-
-
-
-
UDP-N-acetylglucosamine 1-carboxyvinyl-transferase
-
-
-
-
UDP-N-acetylglucosamine enolpyruvyl transferase
-
-
UDP-N-acetylglucosamine enoylpyruvyltransferase
-
-
-
-
UNAG enolpyruvyl transferase
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
carboxyvinyl group transfer
-
-
-
-
SYSTEMATIC NAME
IUBMB Comments
phosphoenolpyruvate:UDP-N-acetyl-D-glucosamine 1-carboxyvinyltransferase
-
CAS REGISTRY NUMBER
COMMENTARY hide
9023-27-2
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
phosphoenolpyruvate + UDP-N-acetyl-alpha-D-glucosamine
phosphate + UDP-N-acetyl-3-O-(1-carboxyvinyl)-alpha-D-glucosamine
show the reaction diagram
-
-
-
-
?
phosphoenolpyruvate + UDP-N-acetyl-D-glucosamine
phosphate + UDP-N-acetyl-3-(1-carboxyvinyl)-D-glucosamine
show the reaction diagram
-
-
-
-
?
phosphoenolpyruvate + UDP-N-acetyl-D-glucosamine
UDP-N-acetyl-3-O-(1-carboxyvinyl)-D-glucosamine + phosphate
show the reaction diagram
-
-
-
-
r
additional information
?
-
-
MurA has also ATPase activity
-
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
phosphoenolpyruvate + UDP-N-acetyl-alpha-D-glucosamine
phosphate + UDP-N-acetyl-3-O-(1-carboxyvinyl)-alpha-D-glucosamine
show the reaction diagram
-
-
-
-
?
phosphoenolpyruvate + UDP-N-acetyl-D-glucosamine
phosphate + UDP-N-acetyl-3-(1-carboxyvinyl)-D-glucosamine
show the reaction diagram
-
-
-
-
?
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1-tuliposide A
-
potent inhibitor
1-tuliposide B
-
potent inhibitor
2-oxo-1,3-benzoxathiol-5-yl (3-chlorophenyl)carbamate
-
-
2-oxo-1,3-benzoxathiol-6-yl benzenesulfonate
-
-
2-oxo-1,3-benzoxathiol-6-yl methanesulfonate
-
-
4,7-dichloro-5-hydroxy-1,3-benzoxathiol-2-one
-
-
5-(prop-2-en-1-yloxy)-1,3-benzoxathiol-2-one
-
-
5-bromo-2-oxo-1,3-benzoxathiol-6-yl phenyl carbonate
-
-
5-hydroxy-1,3-benzoxathiol-2-one
-
-
5-hydroxy-7-(4-methoxyphenyl)-1,3-benzoxathiol-2-one
-
-
5-hydroxynaphtho[1,2-d][1,3]oxathiol-2-one
-
-
Cu2+
-
metal ions do not enhance the activity of enzymes, activity is inhibited by 10 mM
cynaropicrin
-
-
diarylmethane
-
-
Fe2+
-
metal ions do not enhance the activity of enzymes, activity is inhibited by 10 mM
fosfomycin
HESFWYLPHHQSY
-
competitive inhibition
HESFWYLPHQSY
-
i.e. PEP 1354. the peptide seems to prevent the closure of the Pro114-123 loop and, consequently, the open-closed transition of the MurA structure
MnCl2
-
metal ions do not enhance the activity of enzymes, activity is inhibited by 10 mM
PEP 1354 peptide
-
competitive inhibitor
-
pyrazolopyrimidine
-
reversible inhibitor
RWJ-110192
-
reversible inhibitor
RWJ-140998
-
irreversible inhibitor
RWJ-3981
-
irreversible inhibitor
T6361
-
competitive inhibition
T6362
-
competitive inhibition
terreic acid
-
irreversible inhibitor
tulipaline A
-
-
tulipaline B
-
-
Zn2+
-
metal ions do not enhance the activity of enzymes, activity is inhibited by 10 mM
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.00045
phosphoenolpyruvate
0.0178
UDP-N-acetyl-D-glucosamine
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1.8
phosphoenolpyruvate
-
pH and temperature not specified in the publication
1.8 - 2.4
UDP-N-acetyl-D-glucosamine
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.004
phosphoenolpyruvate
-
pH and temperature not specified in the publication
0.000101
UDP-N-acetyl-D-glucosamine
-
pH and temperature not specified in the publication
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.00053 - 0.0045
fosfomycin
0.2
HESFWYLPHQSY
Pseudomonas aeruginosa
-
pH and temperature not specified in the publication
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6 - 9
-
enzyme shows activity at wide range of pH
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
Highest Expressing Human Cell Lines
Cell Line Links Gene Links
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malfunction
-
gram-negative bacteria have only one copy of the murA gene, its deletion is lethal
physiological function
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
A0A8G7Q3E1_PSEAI
421
0
44636
TrEMBL
-
A0A8G2RWP4_PSEAI
421
0
44574
TrEMBL
-
A0A8G2TIA5_PSEAI
421
0
44616
TrEMBL
-
A0A8G2Q2Y5_PSEAI
421
0
44636
TrEMBL
-
A0A3S0J0R5_PSEAI
421
0
44728
TrEMBL
-
A0A643IY33_PSEAI
411
0
43602
TrEMBL
-
A0A8G4A105_PSEAI
421
0
44672
TrEMBL
-
A0A8G3NEH3_PSEAI
421
0
44514
TrEMBL
-
A0A2R3J4E2_PSEAI
421
0
44727
TrEMBL
-
A0A8G7MR17_PSEAI
421
0
44593
TrEMBL
-
A0A8G4GMD7_PSEAI
421
0
44630
TrEMBL
-
A0A8G2RLM5_PSEAI
421
0
44586
TrEMBL
-
A0A071L3S8_PSEAI
421
0
44646
TrEMBL
-
A0A8G5MYW8_PSEAI
421
0
44616
TrEMBL
-
A0A8G2YLY8_PSEAI
421
0
44616
TrEMBL
-
A0A8G7JRK7_PSEAI
421
0
44636
TrEMBL
-
A0A8G3JIE1_PSEAI
421
0
44674
TrEMBL
-
A0A8F9P5X9_PSEAI
421
0
44616
TrEMBL
-
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
89000
-
as fusion protein with maltose binding protein, determined by SDS-PAGE
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
no effect of 10% DMSO on the activity of enzyme
-
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
MurA purification is done by using self packed amylose resin column
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
cloning and expression of MurA using pMAL expression system in frame with the fusion maltose binding protein in Escherichia coli BL21
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
drug development
-
enzyme is an ideal target for the discovery of novel antibiotics against gram-negative pathogens as they have only one copy of murA gene in its genome
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Molina-Lopez, J.; Sanschagrin, F.; Levesque, R.C.
A peptide inhibitor of MurA UDP-N-acetylglucosamine enolpyruvyl transferase: the first committed step in peptidoglycan biosynthesis
Peptides
27
3115-3121
2006
Pseudomonas aeruginosa
Manually annotated by BRENDA team
Dube, S.; Nanda, K.; Rani, R.; Kaur, N.; Nagpal, J.; Upadhyay, D.; Cliffe, I.; Saini, K.; Purnapatre, K.
UDP-N-acetylglucosamine enolpyruvyl transferase from Pseudomonas aeruginosa
World J. Microbiol. Biotechnol.
26
1623-1629
2010
Escherichia coli, Pseudomonas aeruginosa
Manually annotated by BRENDA team
Gautam, A.; Rishi, P.; Tewari, R.
UDP-N-acetylglucosamine enolpyruvyl transferase as a potential target for antibacterial chemotherapy: recent developments
Appl. Microbiol. Biotechnol.
92
211-225
2011
Enterobacter cloacae (P33038), Escherichia coli (P0A749), Mycobacterium tuberculosis (P9WJM1), Mycobacterium tuberculosis H37Rv (P9WJM1), Pseudomonas aeruginosa, Staphylococcus aureus, Streptococcus pneumoniae
Manually annotated by BRENDA team
Lima, A.H.; Dos Santos, A.M.; Alves, C.N.; Lameira, J.
Computed insight into a peptide inhibitor preventing the induced fit mechanism of MurA enzyme from Pseudomonas aeruginosa
Chem. Biol. Drug Des.
89
599-607
2017
Pseudomonas aeruginosa
Manually annotated by BRENDA team