[2] Families of serine peptidases

Rawlings, Neil D.; Barrett, Alan J.

doi:10.1016/0076-6879(94)44004-2

Cited by 629Protease and Inhibitor MechanismsEnzyme Structure and FunctionProtein Structure and Dynamics

[2] Families of serine peptidases

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Rawlings, Neil D., Barrett, Alan J.·1994·Methods in Enzymology

DOI 10.1016/0076-6879(94)44004-2PMC PMC7133253

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Abstract

Publisher Summary This chapter examines families of serine peptidases. Serine peptidases are found in viruses, bacteria, and eukaryotes. They include exopeptidases, endopeptidases, oligopeptidases, and omega peptidases. On the basis of three-dimensional structures, most of the serine peptidase families can be grouped together into about six clans that may have common ancestors. The structures are known for members of four of the clans, chymotrypsin, subtilisin, carboxypeptidase C, and Escherichia D-Ala-D-Ala peptidase A. The peptidases of chymotrypsin, subtilisin, and carboxypeptidase C clans have a common “catalytic triad” of three amino acids—namely, serine (nucleophile), aspartate (electrophile), and histidine (base). The geometric orientations of these are closely similar between families; however the protein folds are quite different. The arrangements of the catalytic residues in the linear sequences of members of the various families commonly reflect their relationships at the clan level. The members of the chymotrypsin family are almost entirely confined to animals. 10 families are included in chymotrypsin clan (SA), and all the active members of these families are endopeptidases. The order of catalytic residues in the polypeptide chain in clan SA is His/Asp/Ser.

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Subtilases: the superfamily of subtilisin-like serine proteases.
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“They are present in many plant tissues, but more abundantly in fruits, and take part in many metabolic pathways of the plant [61].”
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High precision protein functional site detection using 3D convolutional neural networks
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Comparative studies of the specificities of α-chymotrypsin and subtilisin BPN′. Studies with flexible substrates
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On the Evolution of Specificity and Catalysis in SubtilisinPreprint
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Comparative studies of the specificities of α-chymotrypsin and subtilisin BPN′. Studies with flexible and ‘locked’ substrates
Pattabiraman, T. N., & Lawson, W. B. (1972) · Biochemical Journal · doi:10.1042/bj1260659 · Cited by 13 · see citing works

Authors: Rawlings, N. D., & Barrett, A. J.
ORCID: Rawlings, Neil D.
Barrett, Alan J.
Venue: Methods in Enzymology
Publisher: Elsevier
Published: 1994
Volume: 244
Pages: 19-61
ISSN: 0076-6879 (ISSN-L)
DOI: 10.1016/0076-6879(94)44004-2
PMC: PMC7133253
OpenAlex: W1550745757
Semantic Scholar: 0c25d597ecfc252eb8e770eef00ea741a3398751
Cited by: 629
References: 102
Citations by year: 2026: 8 · 2025: 13 · 2024: 17 · 2023: 10 · 2022: 19 · 2021: 22 · 2020: 16 · 2019: 19 · 2018: 16 · 2017: 13 · 2016: 18 · 2015: 21 · 2014: 29 · 2013: 24 · 2012: 46
FWCI: 15.83
Type: book chapter
Language: en
Open access: green
www.ncbi.nlm.nih.gov
Locations: Methods in enzymology on CD-ROM/Methods in enzymology (publishedVersion)
PubMed Central (publishedVersion)
PubMed (publishedVersion)
Topics: Life Sciences › Biochemistry, Genetics and Molecular Biology › Cancer Research › Protease and Inhibitor Mechanisms
Physical Sciences › Materials Science › Materials Chemistry › Enzyme Structure and Function
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Structure and Dynamics
Keywords: serine protease, catalytic triad, protein structure, protein evolution, exopeptidases, endopeptidase, oligopeptidase
MeSH terms: Amino Acid Sequence, Carboxypeptidases, Chymotrypsin, Molecular Sequence Data, Serine Endopeptidases, Subtilisins

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[2] Families of serine peptidases

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