1bfd
From Proteopedia
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BENZOYLFORMATE DECARBOXYLASE FROM PSEUDOMONAS PUTIDA
Overview
The crystal structure of the thiamin diphosphate (ThDP)-dependent enzyme, benzoylformate decarboxylase (BFD), the third enzyme in the mandelate, pathway of Pseudomonas putida, has been solved by multiple isomorphous, replacement at 1.6 A resolution and refined to an R-factor of 15.0% (free, R = 18.6%). The structure of BFD has been compared to that of other, ThDP-dependent enzymes, including pyruvate decarboxylase. The overall, architecture of BFD resembles that of the other family members, and, cofactor- and metal-binding residues are well conserved. Surprisingly, there is no conservation of active-site residues not directly bound to the, cofactor. The position of functional groups in the active site may be, conserved, however. Three classes of metal ions have been identified in, the BFD ... [(full description)]
About this Structure
1BFD is a [Single protein] structure of sequence from [Pseudomonas putida] with CA, MG and TPP as [ligands]. Active as [Benzoylformate decarboxylase], with EC number [4.1.1.7]. Structure known Active Sites: CA1, CA2, MG1 and PP2. Full crystallographic information is available from [OCA].
Reference
The crystal structure of benzoylformate decarboxylase at 1.6 A resolution: diversity of catalytic residues in thiamin diphosphate-dependent enzymes., Hasson MS, Muscate A, McLeish MJ, Polovnikova LS, Gerlt JA, Kenyon GL, Petsko GA, Ringe D, Biochemistry. 1998 Jul 14;37(28):9918-30. PMID:9665697
Page seeded by OCA on Tue Oct 30 12:45:10 2007
Categories: Benzoylformate decarboxylase | Pseudomonas putida | Single protein | Gerlt, J.A. | Hasson, M.S. | Kenyon, G.L. | Mcleish, M.J. | Muscate, A. | Petsko, G.A. | Polovnikova, L.S. | Ringe, D. | CA | MG | TPP | Carbon-carbon | Decarboxylase | Lyase | Mandelate catabolism | Thiamin diphosphate
