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Information on EC 2.3.1.202 - UDP-4-amino-4,6-dideoxy-N-acetyl-beta-L-altrosamine N-acetyltransferase and Organism(s) Helicobacter pylori and UniProt Accession O25094

for references in articles please use BRENDA:EC2.3.1.202
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IUBMB Comments
Isolated from Helicobacter pylori. The enzyme is involved in the biosynthesis of pseudaminic acid.
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This record set is specific for:
Helicobacter pylori
UNIPROT: O25094
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The taxonomic range for the selected organisms is: Helicobacter pylori
The expected taxonomic range for this enzyme is: Bacteria, Archaea
Synonyms
A911_06385, CMP-pseudaminic acid N-acetyltransferase, PsEH, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
CMP-pseudaminic acid N-acetyltransferase
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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.
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
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N-4-acetylation
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-
?
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
21400
x * 21000-22000, SDS-PAGE, x * 21400, calculated
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
x * 21000-22000, SDS-PAGE, x * 21400, calculated
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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
to 2.5 A resolution, space group I222 or I212121, with unit-cell parameters a = 107.8, b = 145.4, c = 166.3 A
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Schoenhofen, I.C.; McNally, D.J.; Brisson, J.; Logan, S.M.
Elucidation of the CMP-pseudaminic acid pathway in Helicobacter pylori: synthesis from UDP-N-acetylglucosamine by a single enzymatic reaction
Glycobiology
16
8C-14C
2006
Helicobacter pylori
Manually annotated by BRENDA team
Liu, Y.; Ud-Din, A.; Roujeinikova, A.
Cloning, purification and preliminary crystallographic analysis of the Helicobacter pylori pseudaminic acid biosynthesis N-acetyltransferase PseH
Acta Crystallogr. Sect. F
70
1276-1279
2014
Helicobacter pylori (O25094), Helicobacter pylori ATCC 700392 (O25094)
Manually annotated by BRENDA team
Ud-Din, A.I.; Liu, Y.C.; Roujeinikova, A.
Crystal structure of Helicobacter pylori pseudaminic acid biosynthesis N-acetyltransferase PseH: implications for substrate specificity and catalysis
PLoS ONE
10
e0115634
2015
Helicobacter pylori (O25094), Helicobacter pylori ATCC 700392 (O25094)
Manually annotated by BRENDA team