The enzymic decarboxylation of oxaloacetate

Krampitz, Lester O.; Werkman, C. H.

doi:10.1042/bj0350595

Cited by 153 publications

(36 citation statements)

References 7 publications

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“…Oxalacetate is decomposed enzymatically t o pyruvate and COz (1)(2)(3)(4)(5). T h e decarboxylation also occurs non-enzymatically by spontaneous and metal-catalyzed processes (6)(7)(8)(9)(10).…”

Section: Introductionmentioning

confidence: 99%

Spontaneous decarboxylation of oxalacetic acid

Tsai¹

1967

Can. J. Chem.

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The kinetic study a t different pH values indicates that the monoanion of oxalacetic acid is the major active species which decarboxylates spontaneously. The decarboxylation of the monoanion is favored by nonpolar solvents. Solvent and isotopic effects suggest that the reaction may proceed via a n intramolecular hydrogen-bonded intermediate a s an activated complex. Infrared spectra which show the formation of a n intramolecular hydrogen bond of oxalacetate in solution are obtained. A plausible mechanism consistent with experimental results is proposed for the spontaneous decarboxylation of oxalacetic acid.

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Section: Introductionmentioning

confidence: 99%

Spontaneous decarboxylation of oxalacetic acid

Tsai¹

1967

Can. J. Chem.

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“…Accordingly, PNA-esterase activity is not enhanced by metal ions (e.g. Mn2, Mg21, Zn2) which in several cases are neccessary for enzymatic decarboxylation [23,24]. Moreover no inhibition of the enzyme is observed in presence of EDTA, which is a typical inhibitor of metal ion dependent decarboxylases [241.…”

Section: Discussionmentioning

confidence: 99%

Characterization of Polyneuridine Aldehyde Esterase, a Key Enzyme in the Biosynthesis of Sarpagine/Ajmaline Type Alkaloids

Pfitzner¹,

Stöckigt²

1983

Planta Med

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Polyneuridine aldehyde esterase (PNA-esterase) was isolated and partially purified from cell suspension cultures of RAUWOLFIA SERPENTINA B ENTH. The exceptionally high substrate specific enzyme catalyses the conversion of the monoterpenoid C (10-) into the C (9-)unit at the stage of polyneuridine aldehyde during the biosynthesis of sarpagine/ajmaline type alkaloids. The enzymatically formed compound is the new, labile indole alkaloid 16-epivellosimine. It is this alkaloid which functions as a branch point of the biogenetic routes leading to sarpagan and ajmalan type alkaloids. PNA-esterase occupies a key position in the biosynthesis of both alkaloid groups.

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“…This possibility was proposed by Menkel et al (29) and was indicated by overexpression of the pyruvate carboxylase gene (40), inactivation of PEP carboxykinase (46), inactivation of citrate and methylcitrate synthases (45), and disruption of the malate:quinone oxidoreductase gene (31). However, there have not been many studies addressing the role of oxaloacetate decarboxylase (ODx), an enzyme that has high levels of activity in different C. glutamicum strains (21) and catalyzes the irreversible decarboxylation of oxaloacetate (25), at this key branch point.…”

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confidence: 99%

Genetic and Functional Analysis of the Soluble Oxaloacetate Decarboxylase from Corynebacterium glutamicum

Klaffl

Eikmanns

2010

J Bacteriol

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Soluble, divalent cation-dependent oxaloacetate decarboxylases (ODx) catalyze the irreversible decarboxylation of oxaloacetate to pyruvate and CO 2 . Although these enzymes have been characterized in different microorganisms, the genes that encode them have not been identified, and their functions have been only poorly analyzed so far. In this study, we purified a soluble ODx from wild-type C. glutamicum about 65-fold and used matrix-assisted laser desorption ionization-time of flight (MALDI-TOF) analysis and peptide mass fingerprinting for identification of the corresponding odx gene. Inactivation and overexpression of odx led to an absence of ODx activity and to a 30-fold increase in ODx specific activity, respectively; these findings unequivocally confirmed that this gene encodes a soluble ODx. Transcriptional analysis of odx indicated that there is a leaderless transcript that is organized in an operon together with a putative S-adenosylmethionine-dependent methyltransferase gene. Biochemical analysis of ODx revealed that the molecular mass of the native enzyme is about 62 ؎ 1 kDa and that the enzyme is composed of two ϳ29-kDa homodimeric subunits and has a K m for oxaloacetate of 1.4 mM and a V max of 201 mol of oxaloacetate converted per min per mg of protein, resulting in a k cat of 104 s ؊1 . Introduction of plasmid-borne odx into a pyruvate kinase-deficient C. glutamicum strain restored growth of this mutant on acetate, indicating that a high level of ODx activity redirects the carbon flux from oxaloacetate to pyruvate in vivo. Consistently, overexpression of the odx gene in an L-lysineproducing strain of C. glutamicum led to accumulation of less L-lysine. However, inactivation of the odx gene did not improve L-lysine production under the conditions tested.Corynebacterium glutamicum is a respirative, Gram-positive soil bacterium that is well suited to industrial amino acid production of, e.g., L-glutamate, L-lysine, and L-valine (4,28). This organism possesses a rather complex phosphoenolpyruvate (PEP)-pyruvate-oxaloacetate node (Fig. 1) compared to model organisms, such as Escherichia coli and Bacillus subtilis (49). Due to the importance of this node for supply of precursors for amino acid synthesis and due to the fact that all enzymes of this node show significant activity in glucose-grown cells (13,17,20,22,42,52), much attention has been focused on identifying targets for metabolic engineering (5,18,24,26,36,39,41,46,47,(56)(57)(58). Optimization of cellular oxaloacetate concentrations seems to be crucial, especially for improving L-lysine production. This possibility was proposed by Menkel et al. (29) and was indicated by overexpression of the pyruvate carboxylase gene (40), inactivation of PEP carboxykinase (46), inactivation of citrate and methylcitrate synthases (45), and disruption of the malate:quinone oxidoreductase gene (31). However, there have not been many studies addressing the role of oxaloacetate decarboxylase (ODx), an enzyme that has high levels of activity in different C. glutami...

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The enzymic decarboxylation of oxaloacetate

Cited by 153 publications

References 7 publications

Spontaneous decarboxylation of oxalacetic acid

Spontaneous decarboxylation of oxalacetic acid

Characterization of Polyneuridine Aldehyde Esterase, a Key Enzyme in the Biosynthesis of Sarpagine/Ajmaline Type Alkaloids

Genetic and Functional Analysis of the Soluble Oxaloacetate Decarboxylase from Corynebacterium glutamicum

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