2.6.1.102: GDP-perosamine synthase

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For detailed information about GDP-perosamine synthase, go to the full flat file.

Reaction

Synonyms

GDP-4-keto-6-deoxy-D-mannose-4-aminotransferase, GDP-perosamine synthase, PerA, RfbE

ECTree

     2 Transferases

         2.6 Transferring nitrogenous groups

             2.6.1 Transaminases

                2.6.1.102 GDP-perosamine synthase

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Results	in table
1	Activating Compound
289	AA Sequence
4	Cloned(Commentary)
4	Cofactor
2	Crystallization (Commentary)
1	Inhibitors
4	kcat/KM [mM/s]
11	KM Value [mM]
1	Metals/Ions
5	Molecular Weight [Da]
7	Natural Substrates/ Products (Substrates)
13	Organism
8	Pathway
5	pH Optimum
2	Protein Variants
3	Purification (Commentary)
1	Reaction
8	Reference
2	Specific Activity [micromol/min/mg]
1	Storage Stability
10	Substrates and Products (Substrate)
4	Subunits
7	Synonyms
1	Systematic Name
2	Temperature Optimum [°C]
2	Temperature Stability [°C]
3	Turnover Number [1/s]

Crystallization

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Crystallization on EC 2.6.1.102 - GDP-perosamine synthase

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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

Caulobacter vibrioides

Q9A9H3

721606

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

Caulobacter vibrioides

Q9A9H3

721608