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Information on EC 2.3.1.129 - acyl-[acyl-carrier-protein]-UDP-N-acetylglucosamine O-acyltransferase and Organism(s) Moraxella catarrhalis and UniProt Accession D5VAW8

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EC Tree
IUBMB Comments
Involved with EC 2.4.1.182, lipid-A-disaccharide synthase, and EC 2.7.1.130, tetraacyldisaccharide 4'-kinase, in the biosynthesis of the phosphorylated glycolipid, Lipid A, in the outer membrane of Gram-negative bacteria.
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This record set is specific for:
Moraxella catarrhalis
UNIPROT: D5VAW8
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Word Map
The taxonomic range for the selected organisms is: Moraxella catarrhalis
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Synonyms
udp-n-acetylglucosamine acyltransferase, lilpxa, udp-n-acetylglucosamine 3-o-acyltransferase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
acyltransferase, uridine diphosphoacetylglucosamine
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UDP-N-acetylglucosamine acyltransferase
uridine diphosphoacetylglucosamine acyltransferase
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Acyl group transfer
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PATHWAY SOURCE
PATHWAYS
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-, -, -, -, -, -
SYSTEMATIC NAME
IUBMB Comments
(3R)-3-hydroxyacyl-[acyl-carrier protein]:UDP-N-acetyl-alpha-D-glucosamine 3-O-(3-hydroxyacyl)transferase
Involved with EC 2.4.1.182, lipid-A-disaccharide synthase, and EC 2.7.1.130, tetraacyldisaccharide 4'-kinase, in the biosynthesis of the phosphorylated glycolipid, Lipid A, in the outer membrane of Gram-negative bacteria.
CAS REGISTRY NUMBER
COMMENTARY hide
105843-69-4
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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
(R)-3-hydroxydodecanoyl-[acyl-carrier protein] + UDP-N-acetyl-alpha-D-galactosamine
[acyl-carrier protein] + UDP-3-O-(3-hydroxydodecanoyl)-N-acetyl-alpha-D-galactosamine
show the reaction diagram
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(R)-3-hydroxydodecanoyl-[acyl-carrier protein] + UDP-N-acetyl-alpha-D-glucosamine
[acyl-carrier protein] + UDP-3-O-(3-hydroxydodecanoyl)-N-acetyl-alpha-D-glucosamine
show the reaction diagram
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additional information
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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
additional information
?
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1-benzoyl-2-(1H-indol-3-ylmethyl)-4-(2-oxo-2-(1-pyrrolidinyl)ethyl)-3-piperidinol
binding energy score of 4.01. In docked pose, the pyrrolidine ring of the molecule is positioned along H120 of chain A and the indole ring is placed towards chain E. It forms hydrogen bonds with H120 (NE atom) and Q156 (OE1 atom), G139 (N backbone) from chain A and G150 (N backbone) of chain E
3-((3-(((3,4-dichlorophenoxy)acetyl)amino)-15-pyridin-1-yl)methyl)benzenesulfonyl fluoride
binding energy score of 4.4. The dichlorophenoxy-acetyl-amino group occupies a position similar to that of the uridine moiety of the nucleotide substrate. The chlorine atom forms hydrophobic interactions with I147, M165 and V129 of chain E whereas the sulfur group forms pi-sulfur interaction with H120 of chain A
erythroskyrin
binding energy score of ?4.17, spans between two subunits of LpxA interacting with Q68 (OE1 and OE2 atom), L70 (N backbone) and H120 (NE2 atom) of chain A and G196 (backbone O), K200 (NZ atom) of chain E
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
84000
gel filtration
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
trimer
3 * 28000, calculated from sequence
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
the residues D69, L70, K71, H117, H120,G138, H139, Q156 from one chain and N193, R199 from the adjacent chain form the active site and play crucial role in substrate positioningand catalysis
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
gene lpxA, DNA and amino acid sequence determination, subcloning in Escherichia coli, wild-type and mutant strains expression analysis
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Peng, D.; Hong, W.; Choudhury, B.P.; Carlson, R.W.; Gu, X.X.
Moraxella catarrhalis bacterium without endotoxin, a potential vaccine candidate
Infect. Immun.
73
7569-7577
2005
Moraxella catarrhalis (Q3BDJ0), Moraxella catarrhalis, Moraxella catarrhalis O35E (Q3BDJ0)
Manually annotated by BRENDA team
Pratap, S.; Kesari, P.; Yadav, R.; Dev, A.; Narwal, M.; Kumar, P.
Acyl chain preference and inhibitor identification of Moraxella catarrhalis LpxA Insight through crystal structure and computational studies
Int. J. Biol. Macromol.
96
759-765
2017
Moraxella catarrhalis (D5VAW8), Moraxella catarrhalis, Moraxella catarrhalis BBH18 (D5VAW8)
Manually annotated by BRENDA team