Abstract

S-Adenosylhomocysteinase. The mechanism of inactivation of SAHase by 2'dAd will be investigated. 2'3H dAd will be synthesized in order to determine whether 3H is released during inactivation. Uniformly labeled C14 2-d'Ad will also be synthesized to determine the fate of the sugar moiety of 2'dAd subsequent to inactivation. B12-Coenzyme. C-5' chirally labeled B12-coenzyme has been synthesized. Experiments will be carried out to determine whether racemization occurs when the coenzyme is bound to the enzyme under anaerobic conditions. This will be done by NMR spectroscopy. 1-P, 5-S-Me-ribose hydrolase. This enzyme will be isolated and its mechanism of action examined. 1-P, 5-S-Me-ribose is derived from S-Me-adenosine. The enzyme will be isolated and purified and its reaction mechanism will be examined. Initial questions to be answered are: Is O2 required? Does the enzyme contain NAD?

  Funding Agency

Agency
National Institute of Health (NIH)
Institute
National Institute of General Medical Sciences (NIGMS)
Type
Research Project (R01)
Project #
5R01GM012633-24
Application #
3268407
Study Section
Biochemistry Study Section (BIO)
Project Start
1977-12-01
Project End
1988-02-29
Budget Start
1986-12-01
Budget End
1988-02-29
Support Year
24
Fiscal Year
1987
Total Cost
Indirect Cost

  Institution

Name
Brandeis University
Department
Type
Schools of Arts and Sciences
DUNS #
616845814
City
Waltham
State
MA
Country
United States
Zip Code
02454

  Publications

Dai, Y; Pochapsky, T C; Abeles, R H (2001) Mechanistic studies of two dioxygenases in the methionine salvage pathway of Klebsiella pneumoniae. Biochemistry 40:6379-87
Dai, Y; Wensink, P C; Abeles, R H (1999) One protein, two enzymes. J Biol Chem 274:1193-5
Prorok, M; Albeck, A; Foxman, B M et al. (1994) Chloroketone hydrolysis by chymotrypsin and N-methylhistidyl-57-chymotrypsin: implications for the mechanism of chymotrypsin inactivation by chloroketones. Biochemistry 33:9784-90
Wray, J W; Abeles, R H (1993) A bacterial enzyme that catalyzes formation of carbon monoxide. J Biol Chem 268:21466-9
Parisi, M F; Abeles, R H (1992) Inhibition of chymotrypsin by fluorinated alpha-keto acid derivatives. Biochemistry 31:9429-35
Hu, L Y; Abeles, R H (1990) Inhibition of cathepsin B and papain by peptidyl alpha-keto esters, alpha-keto amides, alpha-diketones, and alpha-keto acids. Arch Biochem Biophys 281:271-4
Brady, K; Wei, A Z; Ringe, D et al. (1990) Structure of chymotrypsin-trifluoromethyl ketone inhibitor complexes: comparison of slowly and rapidly equilibrating inhibitors. Biochemistry 29:7600-7
Brady, K; Abeles, R H (1990) Inhibition of chymotrypsin by peptidyl trifluoromethyl ketones: determinants of slow-binding kinetics. Biochemistry 29:7608-17
Govardhan, C P; Abeles, R H (1990) Structure-activity studies of fluoroketone inhibitors of alpha-lytic protease and human leukocyte elastase. Arch Biochem Biophys 280:137-46
Abeles, R H; Alston, T A (1990) Enzyme inhibition by fluoro compounds. J Biol Chem 265:16705-8

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