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      The Role of Tyrosine 207 in the Reaction Catalyzed by Saccharomyces cerevisiae phosphoenolpyruvate carboxykinase

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          Abstract

          The functional signifcance of tyrosine 207 of Saccharomyces cerevisiae phosphoenolpyruvate carboxykinase was explored by examining the kinetic properties of the Tyr207Leu mutant. The variant enzyme retained the structural characteristics of the wild-type protein as indicated by circular dichroism, intrinsic fuorescence spectroscopy, and gel-exclusion chromatography. Kinetic analyses of the mutated variant showed a 15-fold increase in Km CO2, a 32fold decrease in Vmax, and a 6-fold decrease in Km for phosphoenolpyruvate. These results suggest that the hydroxyl group of Tyr 207 may polarize CO2 and oxaloacetate, thus facilitating the carboxylation/decarboxylation steps.

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          Structural insights into the mechanism of PEPCK catalysis.

          Todd Holyoak, Daniel Sullivan, T Nowak (2006)
          Phosphoenolpyruvate carboxykinase catalyzes the reversible decarboxylation of oxaloacetic acid with the concomitant transfer of the gamma-phosphate of GTP to form PEP and GDP as the first committed step of gluconeogenesis and glyceroneogenesis. The three structures of the mitochondrial isoform of PEPCK reported are complexed with Mn2+, Mn2+-PEP, or Mn2+-malonate-Mn2+ GDP and provide the first observations of the structure of the mitochondrial isoform and insight into the mechanism of catalysis mediated by this enzyme. The structures show the involvement of the hyper-reactive cysteine (C307) in the coordination of the active site Mn2+. Upon formation of the PEPCK-Mn2+-PEP or PEPCK-Mn2+-malonate-Mn2+ GDP complexes, C307 coordination is lost as the P-loop in which it resides adopts a different conformation. The structures suggest that stabilization of the cysteine-coordinated metal geometry holds the enzyme as a catalytically incompetent metal complex and may represent a previously unappreciated mechanism of regulation. A third conformation of the mobile P-loop in the PEPCK-Mn2+-malonate-Mn2+ GDP complex demonstrates the participation of a previously unrecognized, conserved serine residue (S305) in mediating phosphoryl transfer. The ordering of the mobile active site lid in the PEPCK-Mn2+-malonate-Mn2+ GDP complex yields the first observation of this structural feature and provides additional insight into the mechanism of phosphoryl transfer.
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            Structure and mechanism of phosphoenolpyruvate carboxykinase.

            Louis T J Delbaere, Leslie W. Tari, A Matte … (1997)
            Article 0 comments Cited 16 times – based on 0 reviews     Review now
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              Transition metal-catalyzed nonoxidative decarboxylation reactions.

              Aimin Liu, Hong-Hong Zhang (2006)
              Decarboxylases typically utilize an organic cofactor or a transition metal coupled with dioxygen to activate their substrates. The recent characterization of alpha-amino-beta-carboxymuconate-epsilon-semialdehyde decarboxylase (ACMSD) has revealed that this enzyme adopts a TIM-barrel (beta/alpha)(8) fold and employs a mononuclear transition metal center to decarboxylate the substrate in an oxidant-independent fashion. Thus, ACMSD represents a type of decarboxylation reaction that has been so far uncharacterized in biological systems. Several close homologues of ACMSD were analyzed, including isoorotate decarboxylase (IDCase), 5-carboxyvanillic acid decarboxylase (5-CVD), gamma-resorcylate decarboxylase (gamma-RSD), and 4-oxalomesaconate hydratase (OMAH). These enzymes are involved in the catabolism of tryptophan and vanillate, the biodegradation of hydroxylbenzoates, and the thymidine salvage pathways in certain organisms. They possess the signature sequence motifs of the amidohydrolase superfamily and likely share the same structural and mechanistic characteristics as that of ACMSD. Analysis of the sequence conservation and evolutionary relationship of ACMSD-related proteins suggests an emerging ACMSD protein family that includes ACMSD and ACMSD-like decarboxylases and hydratases with diverse substrate specificities, many of which are poorly understood in regard to their functions and mechanisms. Progress in the biochemical and structural characterization of ACMSD not only sheds light on the active site of this protein family but also promises the elucidation of the detailed catalytic mechanism of these novel transition metal-dependent nonoxidative decarboxylation reactions.
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                Author and article information

                Journal
                Journal ID (publisher-id): bres
                Title: Biological Research
                Abbreviated Title: Biol. Res.
                Publisher: Sociedad de Biología de Chile (Santiago, , Chile )
                ISSN (Print): 0716-9760
                Publication date (Print and electronic): 2010
                Volume: 43
                Issue: 2
                Pages: 191-195
                Affiliations
                [01] Santiago orgnameUniversidad de Santiago de Chile orgdiv1Facultad de Química y Biología Chile ana.jabalquinto@ 123456usach.cl
                Article
                Publisher ID: S0716-97602010000200007 Publisher ID: S0716-9760(10)04300207
                DOI: 10.4067/S0716-97602010000200007
                SO-VID: 2551a317-1542-46b8-b2ca-1c07e46807e0
                License:

                This work is licensed under a Creative Commons Attribution 4.0 International License.

                History
                Date received : 17 August 2009
                Date revision received : 01 January 2010
                Date accepted : 30 March 2010
                Page count
                Figures: 0, Tables: 0, Equations: 0, References: 21, Pages: 5
                Product

                SciELO Chile

                Categories
                Subject: Articles

                Keywords: CO2 interaction,Saccharomyces cerevisiae,Phosphoenolpyruvate carboxykinase
                Data availability:
                Keywords: CO2 interaction, Saccharomyces cerevisiae, Phosphoenolpyruvate carboxykinase

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