Prolyl Aminopeptidase from Serratia marcescens: Cloning of the Enzyme Gene and Crystallization of the Expressed Enzyme.
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概要
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We cloned and sequenced the Serratia marcescens prolyl aminopeptidase (SPAP) gene. Nucleotide sequence analysis revealed an open reading frame of 951 bp, encoding a protein of 317 amino acids with a predicted molecular weight of 36, 083. The expressed enzyme was purified about 90-fold on columns of Toyopearl HW65C and DEAE-Toyopearl, with an activity recovery of 30%. The apparent molecular weight of the purified enzyme was 36, 000 and 38, 000 as estimated by SDS-PAGE and gel filtration, respectively. The enzyme was not inhibited by diisopropyl phosphofluoridate (DFP) or phenylmethylsulfonyl fluoride (PMSF), but was markedly inhibited by 3, 4-dichloroisocoumarin (DCIC). Crystals of the enzyme were grown by the hanging drop vapor diffusion method using PEG6000 as a precipitant at pH 6.5. The crystals are tetragonal with cell dimensions a=b=65.6 Å, and c=169.81 Å, a space group P41212 or P43212, and probably contain one monomer in the asymmetric unit. They diffract to at least 2.22 Å resolution.
- 社団法人 日本生化学会の論文
著者
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Kabashima Tsutomu
School Of Pharmaceutical Sciences Nagasaki University
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Ito Kiyoshi
School Of Pharmaceutical Sciences Nagasaki University
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KITAZONO Ana
School of Pharmaceutical Sciences, Nagasaki University
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Yoshimoto Tadashi
School of Pharamaceutical Sciences, Nagasaki University
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Kitano Atsuko
School of Pharmaceutical Sciences, Nagasaki University
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