Cited by 896Enzyme Production and CharacterizationEnzyme Structure and FunctionProtease and Inhibitor Mechanisms

Subtilases: the superfamily of subtilisin-like serine proteases.

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Siezen, Roland J., Leunissen, Jack A. M.·1997·Protein Science

Abstract

Subtilases are members of the clan (or superfamily) of subtilisin-like serine proteases. Over 200 subtilases are presently known, more than 170 of which with their complete amino acid sequence. In this update of our previous overview (Siezen RJ, de Vos WM, Leunissen JAM, Dijkstra BW, 1991, Protein Eng 4:719-731), details of more than 100 new subtilases discovered in the past five years are summarized, and amino acid sequences of their catalytic domains are compared in a multiple sequence alignment. Based on sequence homology, a subdivision into six families is proposed. Highly conserved residues of the catalytic domain are identified, as are large or unusual deletions and insertions. Predictions have been updated for Ca(2+)-binding sites, disulfide bonds, and substrate specificity, based on both sequence alignment and three-dimensional homology modeling.

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Authors
Siezen, R. J., & Leunissen, J. A. M.
Affiliations
  • Nederlands Instituut Voor Zuivel Oonderzoek (NL)
  • Radboud University Nijmegen (NL)
Corresponding author
Siezen, Roland J.
Venue
Protein Science
Publisher
Wiley
Published
1997-03
Volume
6
Issue
3
Pages
501-523
ISSN
0961-8368 (ISSN-L)
OpenAlex
W2048846412
Cited by
896
References
76
Citations by year
2026: 15 · 2025: 13 · 2024: 20 · 2023: 28 · 2022: 24 · 2021: 20 · 2020: 21 · 2019: 23 · 2018: 27 · 2017: 28 · 2016: 36 · 2015: 22 · 2014: 31 · 2013: 43 · 2012: 49
FWCI
5.67
Type
journal article
Language
en
Open access
Locations
  • Protein Science (publishedVersion)
  • PubMed Central (publishedVersion)
  • PubMed (publishedVersion)
  • Radboud Repository (Radboud University) (submittedVersion)
Funders
Nederlandse Organisatie voor Wetenschappelijk Onderzoek
Topics
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Biotechnology › Enzyme Production and Characterization
  • Physical Sciences › Materials Science › Materials Chemistry › Enzyme Structure and Function
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Cancer Research › Protease and Inhibitor Mechanisms
Keywords
subtilases, subtilisin-like protease, catalytic domain, sequence homology, protein families, conserved residues, indels, calcium binding sites, disulfide bonds, substrate specificity, homology modeling
MeSH terms
Amino Acid Sequence, Animals, Humans, Molecular Sequence Data, Serine Endopeptidases, Sequence Homology, Amino Acid

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