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Information on EC 2.6.1.92 - UDP-4-amino-4,6-dideoxy-N-acetyl-beta-L-altrosamine transaminase and Organism(s) Helicobacter pylori and UniProt Accession O25130

for references in articles please use BRENDA:EC2.6.1.92

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IUBMB Comments

A pyridoxal 5′-phosphate protein. The enzyme transfers the primary amino group of L-glutamate to C-4′′ of UDP-4-dehydro sugars, forming a C-N bond in a stereo configuration opposite to that of UDP. The enzyme from the bacterium Bacillus cereus has been shown to act on UDP-2-acetamido-2,6-dideoxy-β-L-arabino-hex-4-ulose, UDP-β-L-threo-pentapyranos-4-ulose, UDP-4-dehydro-6-deoxy-D-glucose, and UDP-2-acetamido-2,6-dideoxy-α-D-xylo-hex-4-ulose. cf. EC 2.6.1.34, UDP-N-acetylbacillosamine transaminase, which catalyses a similar reaction, but forms the C-N bond in the same stereo configuration as that of UDP.

The taxonomic range for the selected organisms is: Helicobacter pylori
The expected taxonomic range for this enzyme is: Bacteria, Archaea

Synonyms
cj1294, hp0366, more

SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
PATHWAY SOURCE
PATHWAYS
MetaCyc
2-acetamido-4-amino-2,4,6-trideoxy-alpha-D-galactosyl-diphospho-ditrans,octacis-undecaprenol biosynthesis, CMP-pseudaminate biosynthesis, polymyxin resistance, UDP-yelosamine biosynthesis
SYSTEMATIC NAME
IUBMB Comments
UDP-4-amino-4,6-dideoxy-N-acetyl-beta-L-altrosamine:2-oxoglutarate transaminase
A pyridoxal 5'-phosphate protein. The enzyme transfers the primary amino group of L-glutamate to C-4'' of UDP-4-dehydro sugars, forming a C-N bond in a stereo configuration opposite to that of UDP. The enzyme from the bacterium Bacillus cereus has been shown to act on UDP-2-acetamido-2,6-dideoxy-beta-L-arabino-hex-4-ulose, UDP-beta-L-threo-pentapyranos-4-ulose, UDP-4-dehydro-6-deoxy-D-glucose, and UDP-2-acetamido-2,6-dideoxy-alpha-D-xylo-hex-4-ulose. cf. EC 2.6.1.34, UDP-N-acetylbacillosamine transaminase, which catalyses a similar reaction, but forms the C-N bond in the same stereo configuration as that of UDP.
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY hide
Reversibility
r=reversible
ir=irreversible
?=not specified
UDP-2-acetamido-2,6-dideoxy-beta-L-arabino-hex-4-ulose + L-glutamate
UDP-4-amino-4,6-dideoxy-L-N-acetyl-beta-L-altrosamine + 2-oxoglutarate
show the reaction diagram
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY hide
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
UDP-2-acetamido-2,6-dideoxy-beta-L-arabino-hex-4-ulose + L-glutamate
UDP-4-amino-4,6-dideoxy-L-N-acetyl-beta-L-altrosamine + 2-oxoglutarate
show the reaction diagram
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
pyridoxal 5'-phosphate
a pyridoxal 5'-phosphate protein
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
top print hide Go to Organism Search
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
Highest Expressing Human Cell Lines
Cell Line Links Gene Links
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
the enzyme is involved biosynthesis of 5,7-bis(acetylamino)-3,5,7,9-tetradeoxy-L-glycero-alpha-L-manno-2-nonulopyranosonic acid (pseudaminic acid). Helicobacter pylori flagellin is heavily glycosylated with pseudaminic acid. The glycosylation process is essential for assembly of functional flagellar filaments and consequent bacterial motility. Motility is a key virulence factor for this and other important pathogens
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
homodimer
PseC is a homodimer in solution (as shown by dynamic light scattering) as well as in the crystal structure, where the two monomers are related by 2fold crystallographic symmetry. The inter-subunit interactions are extensive, involving several elements of secondary structure, predominantly from the N-terminal domains of both monomers. Each monomer contributes to the active site
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
crystal structure of the native protein, its complexes with pyridoxal 5'-phosphate alone and in combination with UDP-4-amino-4,6-dideoxy-L-N-acetyl-beta-L-altrosamine. A crystal of apo-PseC is obtained in 2 days at 20Ā°C from a hanging drop by mixing 0.0015 ml of protein in buffer with 0.0015 ml of reservoir solution containing 0.2 M ammonium acetate, 0.1 M trisodium citrate, pH 5.6, 30% polyethylene glycol 4000. The crystals belong to space group P2(1)2(1)2 with unit cell dimensions a = 87.7, b = 155.4, and c = 71.5 A and Z = 4
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
medicine
the enzyme is involved biosynthesis of 5,7-bis(acetylamino)-3,5,7,9-tetradeoxy-L-glycero-alpha-L-manno-2-nonulopyranosonic acid (pseudaminic acid). Helicobacter pylori flagellin is heavily glycosylated with pseudaminic acid. The glycosylation process is essential for assembly of functional flagellar filaments and consequent bacterial motility. Because motility is a key virulence factor for this and other important pathogens, the pseudaminic acid biosynthetic pathway offers potential for novel therapeutic targets
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Schoenhofen, I.C.; McNally, D.J.; Vinogradov, E.; Whitfield, D.; Young, N.M.; Dick, S.; Wakarchuk, W.W.; Brisson, J.R.; Logan, S.M.
Functional characterization of dehydratase/aminotransferase pairs from Helicobacter and Campylobacter: enzymes distinguishing the pseudaminic acid and bacillosamine biosynthetic pathways
J. Biol. Chem.
281
723-732
2006
Campylobacter jejuni, Helicobacter pylori (O25130), Helicobacter pylori
Manually annotated by BRENDA team
Schoenhofen, I.C.; Lunin, V.V.; Julien, J.P.; Li, Y.; Ajamian, E.; Matte, A.; Cygler, M.; Brisson, J.R.; Aubry, A.; Logan, S.M.; Bhatia, S.; Wakarchuk, W.W.; Young, N.M.
Structural and functional characterization of PseC, an aminotransferase involved in the biosynthesis of pseudaminic acid, an essential flagellar modification in Helicobacter pylori
J. Biol. Chem.
281
8907-8916
2006
Helicobacter pylori (O25130)
Manually annotated by BRENDA team