The interaction of sulfhydryl and histidine groups of succinyl-CoA synthetase, phosphotransacetylase and carnitine acetyltransferase will be examined. A cyanogen bromide-derived peptide containing the important sulfhydryl group of succinyl-CoA synthetase will be digested with proteolytic enzymes. The peptides of the digest will be examined with regard to their amino acid sequence.

Agency
National Institute of Health (NIH)
Institute
National Institute of General Medical Sciences (NIGMS)
Type
Research Project (R01)
Project #
5R01GM017534-16
Application #
3269130
Study Section
Biochemistry Study Section (BIO)
Project Start
1978-09-01
Project End
1987-08-31
Budget Start
1986-09-01
Budget End
1987-08-31
Support Year
16
Fiscal Year
1986
Total Cost
Indirect Cost
Name
University of Texas Health Science Center San Antonio
Department
Type
Overall Medical
DUNS #
800772162
City
San Antonio
State
TX
Country
United States
Zip Code
78229
Nishimura, J S; Ybarra, J; Mann, C J et al. (1993) Sensitivity of Escherichia coli succinyl-CoA mutants at Trp beta 76 to clostripain and to trypsin. ADP and ATP protect against cleavage by clostripain at Arg beta 80. J Biol Chem 268:13717-22
Luo, G X; Nishimura, J S (1992) Adenosine 5'-tetraphosphate is synthesized by the histidine alpha 142----asparagine mutant of Escherichia coli succinyl-CoA synthetase. J Biol Chem 267:9516-20
Mann, C J; Mitchell, T; Nishimura, J S (1991) Phosphorylation and formation of hybrid enzyme species test the ""half of sites"" reactivity of Escherichia coli succinyl-CoA synthetase. Biochemistry 30:1497-503
Luo, G X; Nishimura, J S (1991) Site-directed mutagenesis of Escherichia coli succinyl-CoA synthetase. Histidine 142 alpha is a facilitative catalytic residue. J Biol Chem 266:20781-5
Nishimura, J S; Mann, C J; Ybarra, J et al. (1990) Intrinsic fluorescence of succinyl-CoA synthetase and four tryptophan mutants. Tryptophan 76 and tryptophan 248 of the beta-subunit are responsive to CoA binding. Biochemistry 29:862-5
Mann, C J; Hardies, S C; Nishimura, J S (1989) Site-directed mutagenesis of Escherichia coli succinyl-CoA synthetase. beta-Cys325 is a nonessential active site residue. J Biol Chem 264:1457-60
Khan, I A; Nishimura, J S (1988) Native-like intermediate on the folding pathway of Escherichia coli succinyl-CoA synthetase. J Biol Chem 263:2152-8
Nishimura, J S; Ybarra, J; Mitchell, T et al. (1988) Isolation, amino acid analyses and refolding of subunits of pig heart succinyl-CoA synthetase. Biochem J 250:429-34
Ybarra, J; Prasad, A R; Nishimura, J S (1986) Chemical modification of tryptophan residues in Escherichia coli succinyl-CoA synthetase. Effect on structure and enzyme activity. Biochemistry 25:7174-8
Nishimura, J S; Mitchell, T (1985) Reaction of substrates with 35S-thiophosphorylated succinyl-CoA synthetase of pig heart. Similarities to the case of the Escherichia coli enzyme. J Biol Chem 260:2077-9