title: [Substrate specificity of phosphoribosyl-aminoimidazole-succinocarboxamide synthetase (SAICAR-synthetase) from Saccharomyces cerevisiae yeast].
abstract: The substrate specificity of phosphoribosyl-aminoimidazole-succinocarboxamide-synthetase (SAICAR-synthetase, EC 6.3.2.6) of the yeast Saccharomyces cerevisiae towards a set of carboxyaminoimidazole ribotide (CAIR) analogs with modifications in the imidazole ring, ribose and phosphate moieties, as well as aspartic acid analogs has been studied. It was found, in particular, that: i) the presence of double charged phosphate group, 2'- and 3'-hydroxyl groups in the ribose fragment and of an amino group in the imidazole ring of the CAIR molecule is not the absolute requirement for the enzymatic reaction; ii) 3'-carboxy-1.2.4-triazole analog of CAIR is a competitive inhibitor of the enzyme; iii) 2'-deoxy-CAIR is a substrate for both yeast SAICAR-synthetase and its avian liver and human erythrocyte counterparts. A new method designed to determine the SAICAR-synthetase activity with the help of bifunctional enzymes possessing, in addition to the SAICAR-synthetase activity, also a phosphoribosyl-aminoimidazole-carboxylase activity, is proposed; this method is based on the use of 2'-deoxy-CAIR. Some aspartic acid analogs (L-malic acid, beta-threo-oxy-, and beta-threo-fluoro-aspartic acids and alanosine) are substrates for yeast SAICAR-synthetase. The possible involvement of malate as an alternative substrate for the SAICAR-synthetase reaction in vivo is discussed. The results of a comparative analysis of already established primary structures of yeast, bacterial, human, and chicken SAICAR-synthetases are presented.
authors.forename: V V
authors.initials: VV
authors.lastname: Alenin
authors.forename: K V
authors.initials: KV
authors.lastname: Ostanin
authors.forename: T R
authors.initials: TR
authors.lastname: Kostikova
authors.forename: V D
authors.initials: VD
authors.lastname: Domkin
authors.forename: V A
authors.initials: VA
authors.lastname: Zubova
authors.forename: M N
authors.initials: MN
authors.lastname: Smirnov
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D001717:Birds; D004912:Erythrocytes / Q000201:enzymology; D006801:Humans; D008969:Molecular Sequence Data; D010453:Peptide Synthases / Q000737:chemistry / Q000378:metabolism*; D012441:Saccharomyces cerevisiae / Q000201:enzymology*; D013379:Substrate Specificity
chemical_list: D010453:Peptide Synthases; C022379:phosphoribosylaminoimidazole-succinocarboxamide synthetase
vernacular_title: Substratnaia spetsifichnost' fosforibozil-aminoimidazol-suktsionokarboksimid-sintetazy (SAIKAR-sintetazy) drozhzheĭ Saccharomyces cerevisiae.