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PMID: 6773768 Published · ppublish English Comparative Study Journal Article

D-glyceraldehyde-3-phosphate dehydrogenase. Amino-acid sequence of the enzyme from the extreme thermophile Thermus aquaticus.

European journal of biochemistry ·Vol. 108 ·No. 2 ·1980-07-00 ·Pages 567-79

Hocking JD, Harris JI

Abstract

1. The amino acid sequence of D-glyceraldehyde-3-phosphate dehydrogenase from the extreme thermophile Thermus aquaticus has been elucidated. 2. The polypeptide contains 332 amino acids and its sequence is 70% identical with that of the enzyme from the moderate thermophile Bacillus stearothermophilus. 3. In contrast to less thermostable forms of the enzymes from B. stearothermophilus, pig, lobster and yeast, the T. aquaticus enzyme has only one cysteine residue, namely cysteine-149 which is required for catalysis.

MeSH Terms
Amino Acid Sequence Amino Acids/analysis Animals Cyanogen Bromide Cysteine/analysis Geobacillus stearothermophilus/enzymology Glyceraldehyde-3-Phosphate Dehydrogenases/analysis Nephropidae/enzymology Pepsin A Peptide Fragments/analysis Swine/metabolism Thermus/enzymology Trypsin Yeasts/enzymology
Chemicals
Amino Acids Peptide Fragments Glyceraldehyde-3-Phosphate Dehydrogenases Trypsin Pepsin A Cysteine Cyanogen Bromide
Authors & Affiliations
2 authors, click to expand affiliations / ORCID
Hocking J D
Harris J I
Article Info
Journal
European journal of biochemistry
Abbr.
Eur J Biochem
ISSN
0014-2956
Published
1980-07-00
Pages
567-79
Language
English
Region
England
NLM ID
0107600
Subset
IM
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