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Crystal structure of prolyl aminopeptidase from Serratia marcescens.

Yoshimoto T, Kabashima T, Uchikawa K, Inoue T, Tanaka N, Nakamura KT, Tsuru M, Ito K
J Biochem 126 559-65 (1999)
Cited: 31 times
EuropePMC logo PMID: 10467172

Abstract

Prolyl aminopeptidase from Serratia marcescens specifically catalyzes the removal of N-terminal proline residues from peptides. We have solved its three-dimensional structure at 2.3 A resolution by the multiple isomorphous replacement method. The enzyme consists of two contiguous domains. The larger domain shows the general topology of the alpha/beta hydrolase fold, with a central eight-stranded beta-sheet and six helices. The smaller domain consists of six helices. The catalytic triad (Ser113, His296, and Asp268) is located near the large cavity at the interface between the two domains. Cys271, which is sensitive to SH reagents, is located near the catalytic residues, in spite of the fact that the enzyme is a serine peptidase. The specific residues which make up the hydrophobic pocket line the smaller domain, and the specificity of the exo-type enzyme originates from this smaller domain, which blocks the N-terminal of P1 proline.

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  3. [Biochemistry and structural biology of microbial enzymes and their medical applications]. Yoshimoto T. Yakugaku Zasshi 127 1035-1045 (2007)

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  18. Crystal structure of the proline iminopeptidase-related protein TTHA1809 from Thermus thermophilus HB8. Okai M, Miyauchi Y, Ebihara A, Lee WC, Nagata K, Tanokura M. Proteins 70 1646-1649 (2008)
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Related citations provided by authors (2)

  1. Prolyl Aminopeptidase from Serratia marcescens : Sequencing and Expression. Kabashima T, Kitazono A, Kitano A, Inoue K, Yoshimoto T J. Biochem. 122 601-605 (1997)
  2. Prolyl aminopeptidase is not a sulfhydryl enzyme: Identification of the active serine residue by site-directed mutagenesis. Kitazono A, Ito K, Yoshimoto T J. Biochem. 116 943-945 (1994)

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