Amino acid sequence of the biotinyl subunit from transcarboxylase.
W. Lee Maloya b c, Botho Bowiena b c, Gene K. Zwolinskia b c, K.G. Kumara b c, H.G. Wooda b c, Lowell H. Ericssona b c, Kenneth A. Walsha b c
- aFrom the Department of Biochemistry, Case Western Reserve University
- bFrom the Department of Biochemistry, University of Washington, Seattle, Washington 98195
- cSchool of Medicine, Cleveland, Ohio 44106
Papers open inside SciRah from the original publisher or repository; SciRah never hosts them.
Abstract
The complete amino acid sequence of the biotinyl subunit from the enzyme transcarboxylase of Propionibacterium shermanii has been determined from the structures of overlapping tryptic and cyanogen bromide peptides together with sequenator analysis on the whole subunit. The subunit contains 123 amino acid residues. Eleven of nineteen residues in the region of biotin attachment, when compared to pyruvate carboxylase from avian liver (Rylatt, D. B., Keech, D. B., and Wallace, J. C. (1977) Arch. Biochem. Biophys. 183, 113-122), were found to be in identical positions relative to biocytin. There was less homology with acetyl-CoA carboxylase from Escherichia coli (Sutton, M. R., Fall, R. R., Nervi, A. M., Alberts, A. W., Vagelos, P. R., and Bradshaw, R. A. (1977) J. Biol. Chem. 252, 3934-3940), but in all of these biotin enzymes there was an alanylmethionyl-biocytinyl-methionine sequence. The secondary structure of the biotinyl subunit has been estimated using the method of Chou and Fasman (Chou, P. Y., and Fasman, G. D. (1978) Adv. Enzymol. 47, 45-148) and considered in relationship to the role of the biotinyl subunit in the structure and function in transcarboxylase.