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Amino Acid Sequence Around the Catalytic Site in Glyceraldehyde-3-Phosphate Dehydrogenase from Bacillus stearothermophilus

By J. Bridgen, J. I. Harris, P. W. McDonald, R. E. Amelunxen and J. R. Kimmel

Abstract

The tryptic peptide containing the active-site cysteine in glyceraldehyde-3-phosphate dehydrogenase from Bacillus stearothermophilus 1503 was isolated after inhibition of the enzyme with 14C-iodoacetate. The amino acid sequence of the 20-residue peptide was determined by 19 successive cycles of dansyl-Edman degradation. The sequence shows considerable homology with its counterparts from mesophilic sources but differs by the addition of Ala-His-His at the N-terminus and by the substitution of phenylalanine for leucine in the prototype sequence

Topics: Enzymology
Year: 1972
OAI identifier: oai:pubmedcentral.nih.gov:251355
Provided by: PubMed Central
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