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Literature summary for 2.6.1.102 extracted from

  • Cook, P.D.; Carney, A.E.; Holden, H.M.
    Accommodation of GDP-linked sugars in the active site of GDP-perosamine synthase (2008), Biochemistry, 47, 10685-10693.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 2.6.1.102

Cloned(Commentary)

Cloned (Comment) Organism
-
 Caulobacter vibrioides

Crystallization (Commentary)

Crystallization (Comment) Organism
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 Caulobacter vibrioides

Inhibitors

Inhibitors Comment Organism Structure
GDP-4-dehydro-6-deoxy-alpha-D-mannose pH 7.5, 22°C Caulobacter vibrioides

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.013
-
 GDP-4-dehydro-6-deoxy-alpha-D-mannose pH 7.5, 22°C Caulobacter vibrioides
0.016
-
 GDP-4-dehydro-3,6-dideoxy-alpha-D-mannose pH 7.5, 22°C Caulobacter vibrioides
0.13
-
 L-glutamate pH 7.5, 22°C, cosubstrate: GDP-4-dehydro-3,6-dideoxy-alpha-D-mannose Caulobacter vibrioides
4.6
-
 L-glutamate pH 7.5, 22°C, cosubstrate: GDP-4-dehydro-6-deoxy-D-mannose Caulobacter vibrioides

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
GDP-4-dehydro-6-deoxy-alpha-D-mannose + L-glutamate Caulobacter vibrioides catalyzes the final step in GDP-perosamine synthesis. L-Perosamine is a component of the O-specific polysaccharide of the lipopolysaccharide component of the outer membrane of Gram-negative bacteria GDP-4-amino-4,6-dideoxy-alpha-D-mannose + 2-oxoglutarate
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 ?

Organism

Organism UniProt Comment Textmining
Caulobacter vibrioides Q9A9H3
-
-

Purification (Commentary)

Purification (Comment) Organism
-
 Caulobacter vibrioides

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
GDP-4-dehydro-3,6-dideoxy-alpha-D-mannose + L-glutamate the unnatural substrate is accommodated in the active site nearly as well as the natural substrate, but the absence of the 3'-OH group affects the alignment of the sugar moiety and, thus, is not properly positioned for efficient catalysis Caulobacter vibrioides GDP-4-amino-3,4,6-trideoxy-alpha-D-mannose + 2-oxoglutarate
-
 ?
GDP-4-dehydro-6-deoxy-alpha-D-mannose + L-glutamate catalyzes the final step in GDP-perosamine synthesis. L-Perosamine is a component of the O-specific polysaccharide of the lipopolysaccharide component of the outer membrane of Gram-negative bacteria Caulobacter vibrioides GDP-4-amino-4,6-dideoxy-alpha-D-mannose + 2-oxoglutarate
-
 ?
GDP-4-dehydro-6-deoxy-alpha-D-mannose + L-glutamate GDP-perosamine synthase can use only L-glutamate as its amino donor Caulobacter vibrioides GDP-4-amino-4,6-dideoxy-alpha-D-mannose + 2-oxoglutarate
-
 ?

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
22
-
 assay at Caulobacter vibrioides

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
0.015
-
 GDP-4-dehydro-3,6-dideoxy-alpha-D-mannose pH 7.5, 22°C Caulobacter vibrioides
2.7
-
 GDP-4-dehydro-6-deoxy-alpha-D-mannose pH 7.5, 22°C Caulobacter vibrioides

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.5
-
 assay at Caulobacter vibrioides

Cofactor

Cofactor Comment Organism Structure
pyridoxal 5'-phosphate a pyridoxal-phosphate protein. The enzyme contains the typically conserved active site lysine residue, which forms a Schiff base with the pyridoxal 5'-phosphate cofactor Caulobacter vibrioides

kcat/KM [mM/s]

kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
208
-
 GDP-4-dehydro-6-deoxy-alpha-D-mannose pH 7.5, 22°C Caulobacter vibrioides