Essential arginine residues in beef kidney D-aspartate oxidase (a preliminary report)
- PMID: 904620
- DOI: 10.1007/BF01732548
Essential arginine residues in beef kidney D-aspartate oxidase (a preliminary report)
Abstract
Partially purified D-aspartate oxidase from beef kidney has been tested in the presence of butanedione or phenylglyoxal, which specifically modify the arginine molecule. The results obtained clearly indicate that arginine residues are involved in the binding of the substrate to the active site of the enzyme.
Similar articles
-
Chemical modification of functional arginyl residues in beef kidney D-aspartate oxidase.Eur J Biochem. 1992 Apr 1;205(1):127-32. doi: 10.1111/j.1432-1033.1992.tb16759.x. Eur J Biochem. 1992. PMID: 1555574
-
Phenol-sulfotransferase inactivation by 2,3-butanedione and phenylglyoxal: evidence for an active site arginyl residue.Biochem Biophys Res Commun. 1977 Oct 10;78(3):1067-73. doi: 10.1016/0006-291x(77)90529-0. Biochem Biophys Res Commun. 1977. PMID: 911328 No abstract available.
-
Essential arginine residues occur in or near the catalytic site of L-amino acid oxidase.Experientia. 1982 May 15;38(5):537-8. doi: 10.1007/BF02327036. Experientia. 1982. PMID: 7095086
-
Inactivation of crystalline tobacco ribulosebisphosphate carboxylase by modification of arginine residues with 2,3-butanedione and phenylglyoxal.Biochim Biophys Acta. 1981 Apr 14;658(2):177-90. doi: 10.1016/0005-2744(81)90288-6. Biochim Biophys Acta. 1981. PMID: 7248300
-
Inactivation of adenylate cyclase by phenylglyoxal and other dicarbonyls. Evidence for existence of essential arginyl residues.Biochim Biophys Acta. 1980 Feb 14;611(2):358-62. doi: 10.1016/0005-2744(80)90072-8. Biochim Biophys Acta. 1980. PMID: 7357013
Cited by
-
[Function of arginine in enzymes].Naturwissenschaften. 1978 Jul;65(7):376-81. doi: 10.1007/BF00439701. Naturwissenschaften. 1978. PMID: 692738 German.
-
Arginyl residues and anion binding sites in proteins.Mol Cell Biochem. 1979 Jul 31;26(2):71-92. doi: 10.1007/BF00232886. Mol Cell Biochem. 1979. PMID: 388184 Review.