NDLI: Argininosuccinate synthetase: essential role of cysteine and arginine residues in relation to structure and mechanism of ATP activation.

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Argininosuccinate synthetase: essential role of cysteine and arginine residues in relation to structure and mechanism of ATP activation.

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Argininosuccinate synthetase: essential role of cysteine and arginine residues in relation to structure and mechanism of ATP activation.

Content Provider	World Health Organization (WHO)-Global Index Medicus
Author	Kumar, S. Lennane, J. Ratner, S.
Abstract	We have undertaken studies to identify amino acid residues that are involved in the catalytic mechanism of argininosuccinate synthetase [L-citrulline:L-aspartate ligase (AMP-forming), EC 6.3.4.5] and have found that a cysteine residue and an arginine residue are required for activity. The reactive cysteine residues are accessible to solvent and available to react with 5,5'-dithiobis(2-nitrobenzoic acid) (DTNB). Four cysteine residues, one per subunit, are shown by enzymatic assay to be required for catalytic activity, suggesting that a reactive cysteine lies within the active site of argininosuccinate synthetase. In the presence of sodium dodecyl sulfate, 12 cysteine residues react with DTNB; consequently, all of the half-cystine residues in the native enzyme are present in the reduced sulfhydryl form. We also present evidence for the participation of arginine groups in the binding of ATP and PPi. Modification of argininosuccinate synthetase with [14C]-phenylglyoxal results in incorporation concomitant with loss of catalytic activity of 4 mol of phenylglyoxal per mol of native enzyme (one arginine per active site). ATP and PPi protect the enzyme from phenylglyoxal incorporation. Based on these results, we propose that the essential arginine in the active site participates in the binding of ATP and PPi. The binding of ATP and PPi at the same site is mutually exclusive; this exclusion is in accord with the finding that argininosuccinate synthetase has one reactive arginine residue per active site per subunit. This is consistent with our previously proposed reaction mechanism.
ISSN	00278424
e-ISSN	10916490
Journal	Proceedings of the National Academy of Sciences of the United States of America
Issue Number	20
Volume Number	82
Language	English
Publisher	National Academy of Sciences
Publisher Date	1985-11-01
Publisher Place	United States
Access Restriction	Open
Subject Keyword	Adenosine Triphosphate Pharmacology Arginine Argininosuccinate Synthase Metabolism Cysteine Ligases Animals Binding Sites Dithionitrobenzoic Acid Enzyme Activation Kinetics Liver Enzymology Phenylglyoxal Protein Binding Research Support, U.S. Gov't, Non-P.H.S. Multidisciplinary
Content Type	Text
Resource Type	Article
Subject	Multidisciplinary

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