|Gene:||gmd||Accession Number: G-9848 (MetaCyc)|
Species: Pseudomonas aeruginosa
Subunit composition of
GDP-D-mannose 4,6-dehydratase = [Gmd]4
GDP-D-mannose 4,6-dehydratase subunit = Gmd
Recombinant GDP-D-mannose 4,6-dehydratase from Pseudomonas aeruginosa has been expressed in Escherichia coli and purified, and the crystal structure has been determined [Webb04]. It is a member of the short-chain dehydrogenase/reductase (SDR) family, NDP-sugar modifying subfamily. Its homotetrameric structure is similar to that of the plant Arabidopsis thaliana enzyme, and differs from most other members of this subfamily, which are homodimers. It has been suggested that this tetrameric, dimer of dimers form may be the active oligomeric state of the enzyme in both prokaryotes and eukaryotes [Webb04].
Gene Citations: [Maki02]
|Map Position: [6,143,109 <- 6,144,080]|
Molecular Weight of Polypeptide: 36.399 kD (from nucleotide sequence)
Enzymatic reaction of: GDP-D-mannose 4,6-dehydratase
Synonyms: GDP-mannose 4,6-dehydratase, Gmd
EC Number: 126.96.36.199
The reaction direction shown, that is, A + B ↔ C + D versus C + D ↔ A + B, is in accordance with the Enzyme Commission system.
The reaction is favored in the direction shown.
GDP-D-Mannose 4,6-dehydratase from Pseudomonas aeruginosa is able to use NADP+ or NAD+ as cofactor in vitro, although NADP(H) remains tightly bound during purification [Webb04].
Maki02: Maki M, Jarvinen N, Rabina J, Roos C, Maaheimo H, Renkonen R, , (2002). "Functional expression of Pseudomonas aeruginosa GDP-4-keto-6-deoxy-D-mannose reductase which synthesizes GDP-rhamnose." Eur J Biochem 269(2);593-601. PMID: 11856318
Webb04: Webb NA, Mulichak AM, Lam JS, Rocchetta HL, Garavito RM (2004). "Crystal structure of a tetrameric GDP-D-mannose 4,6-dehydratase from a bacterial GDP-D-rhamnose biosynthetic pathway." Protein Sci 13(2);529-39. PMID: 14739333
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