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Information on EC 2.5.1.7 - UDP-N-acetylglucosamine 1-carboxyvinyltransferase and Organism(s) Aliivibrio fischeri and UniProt Accession B5F9P4

for references in articles please use BRENDA:EC2.5.1.7
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Aliivibrio fischeri
UNIPROT: B5F9P4 not found.
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Word Map
The taxonomic range for the selected organisms is: Aliivibrio fischeri
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
UDP-N-acetylglucosamine enolpyruvyl transferase
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enoylpyruvate transferase
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enoylpyruvatetransferase
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MurA transferase
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phosphoenolpyruvate-UDP-acetylglucosamine-3-enolpyruvyltransferase
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phosphoenolpyruvate:UDP-2-acetamido-2-deoxy-D-glucose 2-enoyl-1-carboxyethyltransferase
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phosphoenolpyruvate:uridine diphosphate N-acetylglucosamine enolpyruvyltransferase
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phosphoenolpyruvate:uridine-5'-diphospho-N-acetyl-2-amino-2-deoxyglucose-3-enolpyruvyltransferase
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phosphopyruvate-uridine diphosphoacetylglucosamine pyruvatetransferase
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pyruvate-UDP-acetylglucosamine transferase
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pyruvate-uridine diphospho-N-acetyl-glucosamine transferase
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pyruvate-uridine diphospho-N-acetylglucosamine transferase
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pyruvatetransferase, phosphoenolpyruvate-uridine diphosphoacetylglucosamine
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pyruvic-uridine diphospho-N-acetylglucosaminyltransferase
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UDP-N-acetylglucosamine 1-carboxyvinyl-transferase
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UDP-N-acetylglucosamine enolpyruvyl transferase
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UDP-N-acetylglucosamine enoylpyruvyltransferase
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
carboxyvinyl group transfer
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-
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SYSTEMATIC NAME
IUBMB Comments
phosphoenolpyruvate:UDP-N-acetyl-D-glucosamine 1-carboxyvinyltransferase
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CAS REGISTRY NUMBER
COMMENTARY hide
9023-27-2
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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-D-glucosamine
UDP-N-acetyl-3-O-(1-carboxyvinyl)-D-glucosamine + phosphate
show the reaction diagram
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-
-
?
phosphoenolpyruvate + UDP-N-acetyl-D-glucosamine
phosphate + UDP-N-acetyl-3-O-(1-carboxyvinyl)-D-glucosamine
show the reaction diagram
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-
-
?
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-D-glucosamine
phosphate + UDP-N-acetyl-3-O-(1-carboxyvinyl)-D-glucosamine
show the reaction diagram
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-
-
?
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
SwissProt
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
key enzyme is involved in bacterial cell wall peptidoglycan synthesis and a target for the antimicrobial agent fosfomycin, a structural analog of the MurA substrate phosphoenol pyruvate
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
45640
x * 45640, calculated from amino acid sequence
44700
calculated from the 422 amino acids, confirmed by SDS-PAGE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
x * 45640, calculated from amino acid sequence
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
in complex with UDP-N-acetylglucosamine and fosfomycin, sitting drop vapor diffusion method, using 25% (w/v) PEG 3350, 0.1 M bis-Tris pH 6.5
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
Ni-NTA agarose column chromatography and Superdex 75 gel filtration
by metal affinity chromatography with a nickel column
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli BL21 Star (DE3) cells
overexpression in Escherichia coli with a 6-His tag
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
drug development
MurA will be a useful target to identify potential inhibitors of fosfomycin resistance in pharmacological studies
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Kumar, S.; Parvathi, A.; Hernandez, R.L.; Cadle, K.M.; Varela, M.F.
Identification of a novel UDP-N-acetylglucosamine enolpyruvyl transferase (MurA) from Vibrio fischeri that confers high fosfomycin resistance in Escherichia coli
Arch. Microbiol.
191
425-429
2009
Aliivibrio fischeri (B6DVJ7), Aliivibrio fischeri
Manually annotated by BRENDA team
Bensen, D.C.; Rodriguez, S.; Nix, J.; Cunningham, M.L.; Tari, L.W.
Structure of MurA (UDP-N-acetylglucosamine enolpyruvyl transferase) from Vibrio fischeri in complex with substrate UDP-N-acetylglucosamine and the drug fosfomycin
Acta Crystallogr. Sect. F
68
382-385
2012
Aliivibrio fischeri (B5F9P4), Aliivibrio fischeri, Aliivibrio fischeri MJ11 (B5F9P4)
Manually annotated by BRENDA team