Identification of essential arginine residue(s) for Mg-ATP binding of human argininosuccinate synthetase.
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Isashiki Y, Noda T, Kobayashi K, Sase M, Saheki T, Titani K
Identification of essential arginine residue(s) for Mg-ATP binding of human argininosuccinate synthetase.
Protein Seq Data Anal. 1989 Jul;2(4):283-7.
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- 2788888 [ View in PubMed]
- Abstract
Human argininosuccinate synthetase (ASS) activity was found to be inactivated by alpha-dicarbonyls such as 1,2-cyclohexanedione and phenylglyoxal in accordance with pseudo first-order kinetics. The enzyme was almost completely protected from this inactivation by Mg-ATP and partially by its analogues. The strongest protective effect against inactivation was found with Mg-ATP, followed by Mg-ADP, AMP, adenosine and Mg-inorganic pyrophosphate. These results suggest the importance of arginine residue(s) for Mg-ATP binding. We determined the amino acid sequence of the peptide with the highest specific radioactivity derived from ASS which had been labeled with [14C]phenylglyoxal and then cleaved by cyanogen bromide treatment. The sequence obtained, PEFYNRFKGRNDLM, corresponds to residues 148-161 of the amino acid sequence deduced from the cDNA nucleotide sequence determined by Bock et al. [Nucleic Acids Res 11:6505-6512, 1983], and has a high homology with the sequences of ATP-binding sites proposed for several ATP-requiring enzymes.