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PMID: 1270417 Published · ppublish English Comparative Study Journal Article Research Support, U.S. Gov't, Non-P.H.S. Research Support, U.S. Gov't, P.H.S.

Primary structure of streptococcal proteinase. III. Isolation of cyanogen bromide peptides: complete covalent structure of the polypeptide chain.

The Journal of biological chemistry ·Vol. 251 ·No. 7 ·1976-04-10 ·Pages 1955-9

Tai JY, Kortt AA, Liu TY, Elliott SD

Abstract

The following sequence has been derived for streptococcal proteinase. (See article). The sequence permits the assignment of the single cysteine residue essential for catalytic action at position 47 from the NH2 terminus of the protein. The tryptophan residue at the binding site of the enzyme is at position 214. A histidine residue at position 195 has been assigned as the catalytically important entity in the molecule. Streptococcal proteinase and papain, an enzyme with similar properties, are compared with respect to structure and function.

MeSH Terms
Amino Acid Sequence Amino Acids/analysis Binding Sites Cyanogen Bromide Cysteine/analysis Histidine/analysis Papain Peptide Fragments/analysis Peptide Hydrolases Protein Conformation Streptococcus/enzymology Trypsin
Chemicals
Amino Acids Peptide Fragments Histidine Peptide Hydrolases Trypsin Papain Cysteine Cyanogen Bromide
Authors & Affiliations
4 authors, click to expand affiliations / ORCID
Tai J Y
Kortt A A
Liu T Y
Elliott S D
Article Info
Journal
The Journal of biological chemistry
Abbr.
J Biol Chem
ISSN
0021-9258
Published
1976-04-10
Pages
1955-9
Language
English
Region
United States
NLM ID
2985121R
Subset
IM
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