Home LiteratureArticle Details
PMID: 1186854 Published · ppublish English Comparative Study Journal Article Research Support, U.S. Gov't, Non-P.H.S.

Tertiary structural differences between microbial serine proteases and pancreatic serine enzymes.

Nature ·Vol. 257 ·No. 5529 ·1975-10-30 ·Pages 758-63

Delbaere LT, Hutcheon WL, James MN, Thiessen WE

Abstract

Although primary structural homology between bacterial serine proteases and those from the mammalian pancreas is slight, two-thirds of the residues in the bacterial enzyme SGPB as seen at 2.8-A resolution, adopt a similar polypeptide chain conformation to that of the chymotrypsin family. The three major regions of difference show how this family of proteolytic enzymes has developed from the more primitive bacterial to the relatively sophisticated pancreatic enzymes.

MeSH Terms
Amino Acid Sequence Animals Bacteria/enzymology Binding Sites Biological Evolution Chymotrypsin Pancreas/enzymology Pancreatic Elastase Peptide Hydrolases Protein Conformation Serine Structure-Activity Relationship
Chemicals
Serine Peptide Hydrolases Chymotrypsin Pancreatic Elastase
Authors & Affiliations
4 authors, click to expand affiliations / ORCID
Delbaere L T
Hutcheon W L
James M N
Thiessen W E
Article Info
Journal
Nature
Abbr.
Nature
ISSN
0028-0836
Published
1975-10-30
Pages
758-63
Language
English
Region
England
NLM ID
0410462
Subset
IM
Analysis Services
Analysis Services

Contact

No. 2 Wenbo Road, Zhangqiu District, Jinan, Shandong

Qilu Normal University · Genelibs Bioinformatics Lab

750 Shunhua Rd, Jinan

2F, Bldg F, University Science Park

Tel: 0531-88819269

WeChat Official Account

Follow our WeChat subscription account for real-time updates and the latest in medical and biological research.


Business Email

E-mail: [email protected]