Chemical modification of lysine and arginine residues of bovine heart 2-oxoglutarate dehydrogenase: effect on the enzyme activity and regulation. | Zendy

S A Ostrovtsova | Zendy

Open Access

Chemical modification of lysine and arginine residues of bovine heart 2-oxoglutarate dehydrogenase: effect on the enzyme activity and regulation.

Author(s) -

S A Ostrovtsova

Publication year - 1998

Publication title -

acta biochimica polonica

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 0.452

H-Index - 78

eISSN - 1734-154X

pISSN - 0001-527X

DOI - 10.18388/abp.1998_4360

Subject(s) - phenylglyoxal , lysine , chemistry , biochemistry , cofactor , arginine , enzyme , thiamine pyrophosphate , pyridoxal , dehydrogenase , pyridoxal phosphate , pyridoxal 5 phosphate , thiamine , amino acid

Chemical modification of arginine and lysine residues of bovine heart 2-oxoglutarate dehydrogenase with phenylglyoxal and pyridoxal 5'-phosphate inactivated the enzyme, indicating the importance of these residues for the catalysis. Inactivation caused by pyridoxal 5'-phosphate was prevented in the presence of thiamine pyrophosphate and Mg2+ allowing the assumption that lysine residues participate in binding of the cofactor.

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