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Information on EC 2.6.1.87 - UDP-4-amino-4-deoxy-L-arabinose aminotransferase and Organism(s) Escherichia coli and UniProt Accession P77690

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IUBMB Comments
A pyridoxal 5'-phosphate enzyme.
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This record set is specific for:
Escherichia coli
UNIPROT: P77690
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The taxonomic range for the selected organisms is: Escherichia coli
The enzyme appears in selected viruses and cellular organisms
PATHWAY SOURCE
PATHWAYS
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SYSTEMATIC NAME
IUBMB Comments
UDP-4-amino-4-deoxy-beta-L-arabinose:2-oxoglutarate aminotransferase
A pyridoxal 5'-phosphate enzyme.
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
UDP-beta-L-threo-pentapyranos-4-ulose + L-glutamate
UDP-4-amino-4-deoxy-beta-L-arabinose + 2-oxoglutarate
show the reaction diagram
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
UDP-beta-L-threo-pentapyranos-4-ulose + L-glutamate
UDP-4-amino-4-deoxy-beta-L-arabinose + 2-oxoglutarate
show the reaction diagram
ArnB catalyzes the reversible transfer of the amino group from glutamate to the acceptor, uridine 5'-(beta-L-threo-pentapyranosyl-4''-ulose diphosphate), the intermediate that is synthesized by ArnA from UDP-glucuronic acid.the enzyme is highly selective for glutamate as the amine donor, but the equilibrium constant in the direction of UDP-4-amino-4-deoxy-beta-L-arabinose formation is unfavorable
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r
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
pyridoxal 5'-phosphate
the pyridoxal phosphate is converted to the pyridoxamine form in the presence of excess glutamate
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
Uniprot
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
overexpressed using a T7lac promoter-driven construct, hexahistidine-tagged fusion protein
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Breazeale, S.D.; Ribeiro, A.A.; Raetz, C.R.
Origin of lipid A species modified with 4-amino-4-deoxy-L-arabinose in polymyxin-resistant mutants of Escherichia coli. An aminotransferase (ArnB) that generates UDP-4-deoxyl-L-arabinose
J. Biol. Chem.
278
24731-24739
2003
Escherichia coli (P77690)
Manually annotated by BRENDA team