Prolyl aminopeptidase is also present in Enterobacteriaceae: Cloning and sequencing of the Hafnia alvei enzyme-gene and characterization of the expressed enzyme

被引:0
|
作者
Kitazono, A [1 ]
Kitano, A [1 ]
Kabashima, T [1 ]
Ito, K [1 ]
Yoshimoto, T [1 ]
机构
[1] NAGASAKI UNIV,SCH PHARMACEUT SCI,NAGASAKI 852,JAPAN
来源
JOURNAL OF BIOCHEMISTRY | 1996年 / 119卷 / 03期
关键词
aminopeptidase; Hafnia alvei; iminopeptidase; proline;
D O I
暂无
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
The Hafnia alvei prolyl aminopeptidase gene (hpap) was cloned and sequenced, the expressed enzyme (HPAP) was purified to homogeneity and thoroughly characterized, An open reading frame of 1,281 bp was found to code for the enzyme, resulting in a protein of 427 amino acids with a molecular weight of 48,577. HPAP resembles the Aeromonas sobria enzyme, having 45% identity and the same distinctive properties with respect to size and substrate specificities. Both enzymes show similar chromatographic behavior, and HPAP could be purified following the procedure previously described for the Aeromonas enzyme, HPAP was found to be resistant to diisopropylphosphofluoridate as are most of the prolyl aminopeptidases hitherto described, In spite of this similarity, no inhibition by 1 mM p-chloromercuribenzoate solution could be detected, Significant inhibition was, however, observed when the enzyme was incubated with 3,4-dichloroisocoumarin. This study confirms the presence of two types of prolyl aminopeptidases, of which the Hafnia and Aeromonas enzymes constitute one group and the Bacillus, Neisseria, and Lactobacillus enzymes the other, and describes the cloning of the first prolyl aminopeptidase gene from an Enterobacteriaceae.
引用
收藏
页码:468 / 474
页数:7
相关论文
共 42 条
  • [2] Prolyl aminopeptidase from Serratia marcescens: Cloning of the enzyme gene and crystallization of the expressed enzyme
    Kabashima, T
    Kitazono, A
    Kitano, A
    Ito, K
    Yoshimoto, T
    JOURNAL OF BIOCHEMISTRY, 1997, 122 (03): : 601 - 605
  • [3] PROLYL ENDOPEPTIDASE FROM AEROMONAS-HYDROPHILA - CLONING, SEQUENCING, AND EXPRESSION OF THE ENZYME GENE, AND CHARACTERIZATION OF THE EXPRESSED ENZYME
    KANATANI, A
    YOSHIMOTO, T
    KITAZONO, A
    KOKUBO, T
    TSURU, D
    JOURNAL OF BIOCHEMISTRY, 1993, 113 (06): : 790 - 796
  • [4] Prolyl aminopeptidase gene from Flavobacterium meningosepticum: Cloning, purification of the expressed enzyme, and analysis of its sequence
    Kitazono, A
    Kabashima, T
    Huang, HS
    Ito, K
    Yoshimoto, T
    ARCHIVES OF BIOCHEMISTRY AND BIOPHYSICS, 1996, 336 (01) : 35 - 41
  • [5] PROLYL ENDOPEPTIDASE FROM FLAVOBACTERIUM-MENINGOSEPTICUM - CLONING AND SEQUENCING OF THE ENZYME GENE
    YOSHIMOTO, T
    KANATANI, A
    SHIMODA, T
    INAOKA, T
    KOKUBO, T
    TSURU, D
    JOURNAL OF BIOCHEMISTRY, 1991, 110 (06): : 873 - 878
  • [7] CLONING AND EXPRESSION OF AMINOPEPTIDASE-P GENE FROM ESCHERICHIA-COLI HB101 AND CHARACTERIZATION OF EXPRESSED ENZYME
    YOSHIMOTO, T
    MURAYAMA, N
    HONDA, T
    TONE, H
    TSURU, D
    JOURNAL OF BIOCHEMISTRY, 1988, 104 (01): : 93 - 97
  • [8] Dipeptidyl peptidase IV from Xanthomonas maltophilia: Sequencing and expression of the enzyme gene and characterization of the expressed enzyme
    Kabashima, T
    Ito, K
    Yoshimoto, T
    JOURNAL OF BIOCHEMISTRY, 1996, 120 (06): : 1111 - 1117
  • [9] PROTEASE-II FROM MORAXELLA-LACUNATA - CLONING, SEQUENCING, AND EXPRESSION OF THE ENZYME GENE, AND CRYSTALLIZATION OF THE EXPRESSED ENZYME
    YOSHIMOTO, T
    TABIRA, J
    KABASHIMA, T
    INOUE, S
    ITO, K
    JOURNAL OF BIOCHEMISTRY, 1995, 117 (03): : 654 - 660
  • [10] Novel prolyl tri/tetra-peptidyl aminopeptidase from Streptomyces mobaraensis:: Substrate specificity and enzyme gene cloning
    Umezawa, Y
    Yokoyama, K
    Kikuchi, Y
    Date, M
    Ito, K
    Yoshimoto, T
    Matsui, H
    JOURNAL OF BIOCHEMISTRY, 2004, 136 (03): : 293 - 300