Active site cysteinyl and arginyl residues of rhodanese. A novel formation of disulfide bonds in the active site promoted by phenylglyoxal.

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Studies on the active site of rhodanese.

The complete loss of enzymic activity on reaction with alkylating agents, aromatic nitro compounds, or aliphatic mercaptans indicates the importance of sulfhydryl groups for catalysis. Analyses during the course of inactivation with any of these reagents revealed the loss of one of the two -SH groups in the rhodanese monomer when inactivation was complete. Amino acid analysis of iodoacetate-ina...

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Lysine residues involved in the active site

Egg-white avidin was treated with 1 -fluoro-2,4-dinitrobenzene. Modification of an average of one lysine residue per avidin subunit caused the complete loss of biotin binding. Tryptic peptides obtained from the 2,4-dinitrophenylated avidin were fractionated by reversed-phase h.p.l.c. Three peptides contained the 2,4-dinitrophenyl group. Amino acid analysis revealed that lysine residues 45, 94 a...

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ژورنال

عنوان ژورنال: Journal of Biological Chemistry

سال: 1978

ISSN: 0021-9258

DOI: 10.1016/s0021-9258(17)34369-7