The ubiquitous cofactor NADH protects against substrate-induced inhibition of a pyridoxal enzyme

Protein Science

Volumn 5, Issue 12, 1996, Pages 2545-2551

  Jones, Wanda M ^b   Van Ophem, Peter W ^a   Pospischil, Maria A ^b   Ringe, Dagmar ^c   Petsko, Gregory ^c   Soda, Kenji ^d   Manning, James M ^a  

^a NORTHEASTERN UNIVERSITY   (United States)

^b ROCKEFELLER UNIVERSITY   (United States)

^c BRANDEIS UNIVERSITY   (United States)

^d KYOTO UNIVERSITY   (Japan)

Author keywords

D amino acids; enzyme; enzyme inhibition; NADH; transaminase

Indexed keywords

AMINOTRANSFERASE; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE; UBIQUITIN CONJUGATING ENZYME;

AMINO ACID METABOLISM; ARTICLE; CHOLESTEROL SYNTHESIS; CONFORMATIONAL TRANSITION; DECARBOXYLATION; DISSOCIATION CONSTANT; ENZYME ACTIVITY; ENZYME INHIBITION; ENZYME SUBSTRATE; GENE TARGETING; NONHUMAN; OXIDATION REDUCTION REACTION; PRIORITY JOURNAL; PROTEIN CONFORMATION;

EID: 0030465379     PISSN: 09618368     EISSN: None     Source Type: Journal    
DOI: 10.1002/pro.5560051217     Document Type: Article

References (33)

1. Almo SC, Smith DL, Danishefsky AT, Ringe D. 1994. The structural basis for the altered substrate specificity of the R292D active site mutant of aspartate aminotransferase from E. coli. Protein Eng 7.405-412.
2. Bhatia MB, Martinez del Pozo A, Ringe D, Yoshimura T, Soda K, Manning JM 1993. Role reversal for substrates and inhibitors: Inactivation of D-amino acid transaminase by its normal substrates and protection by inhibitors. J Biol Chem 268:17687-17694.
3. Braunstein AE. 1973. Transaminases. In: The Enzymes 9, 3rd ed. p 379.
4. Christen P, Metzler DE. 1985. Transaminases. New York: John Wiley and Sons p 15.
5. Dixon M, Webb EC. 1979. In: Enzymes, 3rd ed. Academic Press. p 476.
6. Futaki S, Ueno H, Martinez del Pozo A, Pospischil MA, Ringe D, Stoddard B, Tanizawa K, Yoshimura T, Soda K, Manning JM. 1990. Substitution of glutamine for lysine at the pyridoxal phosphate binding site of bacterial D-amino acid transaminase leads to an active but attenuated enzyme: Effects of exogenous amines on the slow formation of intermediates. J Biol Chem 265:22306-22312
7. Gale EF, Cundliffe E, Reynolds PE, Richmond MH, Waring MJ. 1981. Biochemical targets for drug action. In: The Molecular Basis of Antibiotic Action, 2nd ed. London: John Wiley & Sons. pp 23-48.
8. Graber R, Kasper P, Malashkevich VN, Sandmeier E, Berger P, Gehring H, Jansonius JN, Christen P. 1995 Changing the reaction specificity of a pyridoxal-5′-phosphate-dependent enzyme. Eur J Biochem 252:686-690.
9. Gray HB, Winkler JR 1996 Electron transfer in proteins. Annu Rev Biochem 65:537-561.
10. Hillar A, Nicholls R 1992. Mechanism for NADPH inhibition of catalase compound II formation. FEBS Lett 314:179-182.
11. Huber R. 1990. A structural basis of light energy and electron transfer in biology. Eur J Biochem 187:283-305.
12. Jones WM, Ringe D, Soda K, Manning JM. 1994. Determination of tree D-amino acids with a bacterial transaminase: Their depletion leads to inhibition of bacterial growth Anal Biochem 218:204-209.
13. Jones WM, Soper TS, Ueno H, Manning JM. 1985. Bacterial D-amino acid transaminase. Methods Enzymol 113:108-113.
14. Jouve HM, Beaumont F, Leger I, Foray J, Pelmont J. 1989. Tightly bound NADPH in Proteus mirabilis PR catalase. Biochem Cell Biol 67:271-271.
15. Kirkman HN, Gaetani GT. 1984. Catalase: A tetrameric enzyme with four tightly bound molecules of NADPH. Proc Natl Acad Sci USA 81:4343-4347.
16. Manning JM, Khomutov RM, Fasella P. 1968. The reaction of β-chloroglutamic acid with glutamate-aspartate transaminase. Eur J Biochem 5:109.
17. Manning JM, Merrifield NE, Jones WM, Gotschlich EC. 1974. Inhibition of bacterial growth by β-chloro-D-alanine. Proc Natl Acad Sci USA 71:417-421.
18. Martinez-Carrion M, Jenkins WT. 1965. D-alanine-D-glutamate transaminase. J Biol Chem 240:3538-3552.
19. Martinez del Pozo A, Merola M, Ueno H, Manning JM, Tanizawa K, Nishimura K, Soda K, Ringe D. 1989a Stereochemistry of reactions catalyzed by bacterial D-amino acid transaminase. J Biol Chem 264:17784-17789.
20. Martinez del Pozo A, Pospischil MA, Ueno H, Tanizawa K, Nishimura K, Soda K, Ringe D, Petsko G. 1989b. Effects of D-senne on bacterial D-amino acid transaminase: Accumulation of an intermediate and inactivation of the enzyme. Biochemistry 28:8798.
21. Martinez del Pozo A, Yoshimura T, Bharia MB, Futaki S, Manning JM. 1992. Inactivation of dimeric D-amino acid transaminase by its normal substrate through coenzyme immobilization in one subunit. Biochemistry 31:6018-6023.
22. Meister A, Sober HA, Tice SV. 1951. Enzymatic decarboxylation of aspartic acid to α-L-alanine. J Biol Chem 189:577-590.
23. Mildvan AS, Leigh RA. 1964. Determination of co-factor dissociation constants from the kinetics of inhibition of enzymes. Biochim Biophys Acta 89:393-397.
24. Miles EW. 1985. Transamination as a side reaction of other phosphopyridoxal enzymes. Christen P, Metzler D, eds. Transaminases. New York: John Wiley & Sons. pp 470-481.
25. Nishimura JS, Manning JM, Meister A. 1962. Studies on the mechanism of activation of aspartic acid β-decarboxylase by α-keto acids and pyridoxal-5′-phosphate. Biochemistry 1:442.
26. Novogrodsky A, Nishimura JS, Meister A. 1963. Transamination and β-decarboxylation of asparte catalyzed by the same pyridoxal enzyme. J Biol Chem 238:(preliminary communication)1903-1905.
27. Soda K, Tanizawa K. 1979. Adv Enzymol 49:1.
28. Soper TS, Jones WM, Lerner B, Trop M, Manning JM. 1977. Inactivation of bacterial D-amino acid transaminase by β-chloro-D-alanine. J Biol Chem 252:3170-3175.
29. Soper TS, Manning JM. 1978. β-Elimination of β-halo substrates by D-amino acid transaminase associated with inactivation of the enzyme. Trapping of a key intermediate in the reaction. Biochemistry 17:3377-3384.
30. Sugio S, Petsko GA, Manning JM, Soda K, Ringe D. 1995. Crystal structure of a D-amino acid aminotransferase: How the protein controls stereoselectivity. Biochemistry 34:9661-9669.
31. Yankeelov JA, Koshland DE. 1965. Evidence for conformational changes induced by substrates of phosphoglucomutase. J Biol Chem 240:1593-1602.
32. Yoshimura T, Bhatia MB, Manning JM, Ringe D, Soda K. 1992. Bacterial D-amino acid transaminase with an asparagine substituted for the active site lysine retains significant catalytic activity: Implications for the role of lysine attached to coenzyme PLP. Biochemistry 31:11748-11754.
33. Yoshimura T, Jhee KH, Soda K. 1996. Stereospecificity for the hydrogen transfer and molecular evolution of pyridoxal enzymes. Biosci Biotech Biochem 60:181-187.