Complete Amino Acid Sequence of Scytalidium lignicolum Acid Protease B

The acid protease B (SLB) of Scytalidium lignicolum was reduced and carboxymethylated and then subjected to tryptic digestion. Five fragments were isolated and some of them were further digested with α-chymotrypsin, thermolysin, and dilute acetic acid. The sequence analysis of these fragments and th...

Full description

Saved in:
Bibliographic Details
Published in:Journal of biochemistry (Tokyo) 1984-01, Vol.95 (2), p.465-475
Main Authors: MAITA, Tetsuo, NAGATA, Shuichi, MATSUDA, Genji, MARUTA, Shinsaku, ODA, Kohei, MURAO, Sawao, TSURU, Daisuke
Format: Article
Language:English
Subjects:
Amino Acid Sequence
Analytical, structural and metabolic biochemistry
Aspartic Acid Endopeptidases
Biological and medical sciences
Chymotrypsin
Disulfides - analysis
Endopeptidases
Enzymes and enzyme inhibitors
Fundamental and applied biological sciences. Psychology
Hydrolases
Hydrolysis
Mitosporic Fungi - enzymology
Peptide Fragments - analysis
proteinase
Scytalidium lignicolum
Online Access:Get full text
Tags: Add Tag
No Tags, Be the first to tag this record!
Description
Summary:The acid protease B (SLB) of Scytalidium lignicolum was reduced and carboxymethylated and then subjected to tryptic digestion. Five fragments were isolated and some of them were further digested with α-chymotrypsin, thermolysin, and dilute acetic acid. The sequence analysis of these fragments and the peptides by conventional methods established the complete amino acid sequence of SLB. The enzyme was composed of 204 amino acid residues with threonine and valine as its amino-and carboxyl-termini, respectively. Locations of three disulfide bridges were also established to be Cys47–126, Cys140–163, and Cys192–201 by enzymatic fragmentation of the denatured and unmodified SLB. Only a slight homology was found in the sequences of SLB and other acid proteases hitherto reported.
ISSN:0021-924X
1756-2651
DOI:10.1093/oxfordjournals.jbchem.a134628