Rabbit liver microsomal endopeptidase with substrate specificity for processing proproteins is structurally related to rat testes metalloendopeptidase 24.15

S. I. Kawabata, K. Nakagawa, T. Muta, S. Iwanaga, E. W. Davie

研究成果: ジャーナルへの寄稿記事

32 引用 (Scopus)

抄録

The detergent extract of rabbit liver microsomes contains an endopeptidase (MEP) with substrate specificity for peptides containing Arg residues at the P1 and P4 positions in the cleavage site (Kawabata, S., and Davie, E. W. (1992) J. Biol. Chem. 267, 10331-10336). These sequences occur in many proproteins such as the vitamin K-dependent proproteins and prohormones. A cDNA coding for MEP has been obtained from three overlapping clones isolated from two rabbit liver λgt10 cDNA libraries. The longest open reading frame of the 3507-base pair cDNA codes for a protein of 704 amino acids, of which 406 residues were confirmed by amino acid sequence analysis. MEP contains a putative active site of -His-Glu-X-X-His-, which is typical of mammalian zinc metallopeptidases. Based on a hydropathy plot, MEP is a hydrophilic protein with no transmembrane domain and no NH2-terminal signal sequence. Amino acid sequence analysis identified Asn at the three potential N-glycosylation sites in the enzyme, indicating that MEP contains no N-linked sugar. MEP is homologous with rat testes metalloendopeptidase 24.15 (60% identity), rat mitochondrial intermediate peptidase (24% identity), Escherichia coli dipeptidyl carboxypeptidase (25% identity), and the open reading frame YCL57w present in yeast chromosome III (35% identity).

元の言語英語
ページ(範囲)12498-12503
ページ数6
ジャーナルJournal of Biological Chemistry
268
発行部数17
出版物ステータス出版済み - 1 1 1993

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thimet oligopeptidase
Endopeptidases
Protein Sequence Analysis
Substrate Specificity
Liver
Open Reading Frames
Testis
Rats
Complementary DNA
Rabbits
Amino Acids
Vitamin K
Metalloproteases
Liver Microsomes
Substrates
Protein Sorting Signals
Processing
Gene Library
Glycosylation
Base Pairing

All Science Journal Classification (ASJC) codes

  • Biochemistry
  • Molecular Biology
  • Cell Biology

これを引用

Rabbit liver microsomal endopeptidase with substrate specificity for processing proproteins is structurally related to rat testes metalloendopeptidase 24.15. / Kawabata, S. I.; Nakagawa, K.; Muta, T.; Iwanaga, S.; Davie, E. W.

:: Journal of Biological Chemistry, 巻 268, 番号 17, 01.01.1993, p. 12498-12503.

研究成果: ジャーナルへの寄稿記事

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abstract = "The detergent extract of rabbit liver microsomes contains an endopeptidase (MEP) with substrate specificity for peptides containing Arg residues at the P1 and P4 positions in the cleavage site (Kawabata, S., and Davie, E. W. (1992) J. Biol. Chem. 267, 10331-10336). These sequences occur in many proproteins such as the vitamin K-dependent proproteins and prohormones. A cDNA coding for MEP has been obtained from three overlapping clones isolated from two rabbit liver λgt10 cDNA libraries. The longest open reading frame of the 3507-base pair cDNA codes for a protein of 704 amino acids, of which 406 residues were confirmed by amino acid sequence analysis. MEP contains a putative active site of -His-Glu-X-X-His-, which is typical of mammalian zinc metallopeptidases. Based on a hydropathy plot, MEP is a hydrophilic protein with no transmembrane domain and no NH2-terminal signal sequence. Amino acid sequence analysis identified Asn at the three potential N-glycosylation sites in the enzyme, indicating that MEP contains no N-linked sugar. MEP is homologous with rat testes metalloendopeptidase 24.15 (60{\%} identity), rat mitochondrial intermediate peptidase (24{\%} identity), Escherichia coli dipeptidyl carboxypeptidase (25{\%} identity), and the open reading frame YCL57w present in yeast chromosome III (35{\%} identity).",
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