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. 1972 Sep;111(3):797-800.
doi: 10.1128/jb.111.3.797-800.1972.

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

J Bridgen  1 , J I Harris, P W McDonald, R E Amelunxen, J R Kimmel
Affiliations

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

J Bridgen et al. J Bacteriol. 1972 Sep.

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 (14)C-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.

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