1w2i
From Proteopedia
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CRYSTAL STRUCTUORE OF ACYLPHOSPHATASE FROM PYROCOCCUS HORIKOSHII COMPLEXED WITH FORMATE
Overview
Acylphosphatases catalyze the hydrolysis of the carboxyl-phosphate bond in, acyl phosphates. Although acylphosphatase-like sequences are found in all, three domains of life, no structure of acylphosphatase has been reported, for bacteria and archaea so far. Here, we report the characterization of, enzymatic activities and crystal structure of an archaeal acylphosphatase., A putative acylphosphatase gene (PhAcP) was cloned from the genomic DNA of, Pyrococcus horikoshii and was expressed in Escherichia coli. Enzymatic, parameters of the recombinant PhAcP were measured using benzoyl phosphate, as the substrate. Our data suggest that, while PhAcP is less efficient, than other mammalian homologues at 25 degrees C, the thermophilic enzyme, is fully active at the optimal growth temperature (98 ... [(full description)]
About this Structure
1W2I is a [Single protein] structure of sequence from [Pyrococcus horikoshii] with FMT as [ligand]. Active as [Acylphosphatase], with EC number [3.6.1.7]. Structure known Active Site: AC1. Full crystallographic information is available from [OCA].
Reference
Crystal structure of a hyperthermophilic archaeal acylphosphatase from Pyrococcus horikoshii--structural insights into enzymatic catalysis, thermostability, and dimerization., Cheung YY, Lam SY, Chu WK, Allen MD, Bycroft M, Wong KB, Biochemistry. 2005 Mar 29;44(12):4601-11. PMID:15779887
Page seeded by OCA on Tue Oct 30 16:22:50 2007
Categories: Acylphosphatase | Pyrococcus horikoshii | Single protein | Allen, M.D. | Bycroft, M. | Cheung, Y.Y. | Chu, W.K. | Lam, S.Y. | Wong, K.B. | FMT | Amyloid | Phosphatase | Stability | Thermophilic
