Information on EC 2.3.1.202 - UDP-4-amino-4,6-dideoxy-N-acetyl-beta-L-altrosamine N-acetyltransferase

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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
2.3.1.202
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RECOMMENDED NAME
GeneOntology No.
UDP-4-amino-4,6-dideoxy-N-acetyl-beta-L-altrosamine N-acetyltransferase
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
acetyl-CoA + UDP-4-amino-4,6-dideoxy-N-acetyl-beta-L-altrosamine = CoA + UDP-2,4-diacetamido-2,4,6-trideoxy-beta-L-altropyranose
show the reaction diagram
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
CMP-pseudaminate biosynthesis
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Amino sugar and nucleotide sugar metabolism
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SYSTEMATIC NAME
IUBMB Comments
acetyl-CoA:UDP-4-amino-4,6-dideoxy-N-acetyl-beta-L-altrosamine N-acetyltransferase
Isolated from Helicobacter pylori. The enzyme is involved in the biosynthesis of pseudaminic acid.
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
subsp. jejuni
UniProt
Manually annotated by BRENDA team
subsp. jejuni
UniProt
Manually annotated by BRENDA team
Helicobacter pylori ATCC 700392
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UniProt
Manually annotated by BRENDA team
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
acetyl-CoA + UDP-4-amino-4,6-dideoxy-N-acetyl-beta-L-altrosamine
CoA + UDP-2,4-diacetamido-2,4,6-trideoxy-beta-L-altropyranose
show the reaction diagram
PDB
SCOP
CATH
ORGANISM
UNIPROT
Helicobacter pylori (strain ATCC 700392 / 26695)
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
PseH alone and in complex with AcCoA, to 1.95 A resolution. PseH folds into a single-domain structure of a central beta-sheet decorated by four alpha-helices with two continuously connected grooves. A deep groove accommodates the AcCoA molecule. The acetyl end of AcCoA points toward an open space in a neighboring shallow groove, which is occupied by extra electron density that potentially serves as a pseudosubstrate. PseH may utilize a catalytic mechanism of acetylation different from other glycosylation-associated acetyltransferases
in complex with cofactor acetyl-CoA, to 2.3 A resolution. PseH is a homodimer in the crystal, each subunit of which has a central twisted beta-sheet flanked by five alpha-helices. The cofactor-binding site is located between the splayed strands beta4 and beta5. The catalytic mechanism involves direct acetyl transfer from AcCoA without an acetylated enzyme intermediate. Modeling of the Michaelis complex suggests that the nucleotide- and 4-amino-4,6-dideoxy-beta-L-AltNAc-binding pockets form extensive interactions with the substrate and are thus the most significant determinants of substrate specificity. A hydrophobic pocket accommodating the 6'-methyl group of the altrose dictates preference to the methyl over the hydroxyl group
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to 2.5 A resolution, space group I222 or I212121, with unit-cell parameters a = 107.8, b = 145.4, c = 166.3 A
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