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Information on EC 2.6.1.102 - GDP-perosamine synthase and Organism(s) Caulobacter vibrioides and UniProt Accession Q9A9H3

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EC Tree
     2 Transferases
         2.6 Transferring nitrogenous groups
             2.6.1 Transaminases
                2.6.1.102 GDP-perosamine synthase
IUBMB Comments
A pyridoxal 5'-phosphate enzyme. D-Perosamine is one of several dideoxy sugars found in the O-specific polysaccharide of the lipopolysaccharide component of the outer membrane of Gram-negative bacteria. The enzyme catalyses the final step in GDP-alpha-D-perosamine synthesis.
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Caulobacter vibrioides
UNIPROT: Q9A9H3
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The taxonomic range for the selected organisms is: Caulobacter vibrioides
The expected taxonomic range for this enzyme is: Bacteria, Archaea
Synonyms
gdp-perosamine synthase, gdp-4-keto-6-deoxy-d-mannose-4-aminotransferase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
GDP-perosamine synthase
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-
SYSTEMATIC NAME
IUBMB Comments
GDP-4-amino-4,6-dideoxy-alpha-D-mannose:2-oxoglutarate aminotransferase
A pyridoxal 5'-phosphate enzyme. D-Perosamine is one of several dideoxy sugars found in the O-specific polysaccharide of the lipopolysaccharide component of the outer membrane of Gram-negative bacteria. The enzyme catalyses the final step in GDP-alpha-D-perosamine synthesis.
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
GDP-4-dehydro-3,6-dideoxy-alpha-D-mannose + L-glutamate
GDP-4-amino-3,4,6-trideoxy-alpha-D-mannose + 2-oxoglutarate
show the reaction diagram
GDP-4-dehydro-6-deoxy-alpha-D-mannose + L-glutamate
GDP-4-amino-4,6-dideoxy-alpha-D-mannose + 2-oxoglutarate
show the reaction diagram
GDP-4-dehydro-6-deoxy-alpha-D-mannose + L-glutamate
GDP-4-amino-4,6-dideoxy-alpha-D-mannose + 2-oxoglutarate
show the reaction diagram
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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
GDP-4-dehydro-6-deoxy-alpha-D-mannose + L-glutamate
GDP-4-amino-4,6-dideoxy-alpha-D-mannose + 2-oxoglutarate
show the reaction diagram
GDP-4-dehydro-6-deoxy-alpha-D-mannose + L-glutamate
GDP-4-amino-4,6-dideoxy-alpha-D-mannose + 2-oxoglutarate
show the reaction diagram
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-
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
pyridoxal 5'-phosphate
pyridoxal 5'-phosphate
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pyridoxal 5'-phosphate-dependent enzyme
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
GDP-4-dehydro-6-deoxy-alpha-D-mannose
pH 7.5, 22°C
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.016
GDP-4-dehydro-3,6-dideoxy-alpha-D-mannose
pH 7.5, 22°C
0.013
GDP-4-dehydro-6-deoxy-alpha-D-mannose
pH 7.5, 22°C
0.13 - 4.6
L-glutamate
0.013
GDP-4-dehydro-6-deoxy-alpha-D-mannose
-
pH 7.5, 22°C
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.015
GDP-4-dehydro-3,6-dideoxy-alpha-D-mannose
pH 7.5, 22°C
2.7
GDP-4-dehydro-6-deoxy-alpha-D-mannose
pH 7.5, 22°C
2.7
GDP-4-dehydro-6-deoxy-alpha-D-mannose
-
pH 7.5, 22°C
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
208
GDP-4-dehydro-6-deoxy-alpha-D-mannose
pH 7.5, 22°C
208
GDP-4-dehydro-6-deoxy-alpha-D-mannose
-
pH 7.5, 22°C
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
hanging drop method of vapor diffusion using a sparse matrix screen. Two crystal structures: a site-directed mutant protein (K186A) complexed with GDP-perosamine and the wild-type enzyme complexed with an unnatural ligand, GDP-3-deoxyperosamine. These structures, determined to 1.6 and 1.7 A resolution, respectively
the three-dimensional structure of the enzyme is determined to a nominal resolution of 1.8 A and refined to an R-factor of 17.9%. Each subunit of the dimeric enzyme contains a seven-stranded mixed beta-sheet, a two-stranded antiparallel beta-sheet, and 12 alpha-helices
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
K186H
-
single mutant enzyme has no detectable catalytic activity with its sugar substrate
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Cook, P.D.; Carney, A.E.; Holden, H.M.
Accommodation of GDP-linked sugars in the active site of GDP-perosamine synthase
Biochemistry
47
10685-10693
2008
Caulobacter vibrioides (Q9A9H3), Caulobacter vibrioides
Manually annotated by BRENDA team
Cook, P.D.; Holden, H.M.
GDP-perosamine synthase: structural analysis and production of a novel trideoxysugar
Biochemistry
47
2833-2840
2008
Caulobacter vibrioides (Q9A9H3), Caulobacter vibrioides
Manually annotated by BRENDA team
Cook, P.D.; Kubiak, R.L.; Toomey, D.P.; Holden, H.M.
Two site-directed mutations are required for the conversion of a sugar dehydratase into an aminotransferase
Biochemistry
48
5246-5253
2009
Caulobacter vibrioides, Caulobacter vibrioides CB15
Manually annotated by BRENDA team