Coenzyme specificity in aldehyde dehydrogenase

Perozich, John; Kuo, Ingrid; Lindahl, Ronald; Hempel, John

doi:10.1016/s0009-2797(00)00227-1

Cited by 26 publications

(18 citation statements)

References 22 publications

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“…It remains to be investigated whether PhnY possesses similar relaxed substrate specificity, but we have determined that PhnY is only active in the presence of an NAD ϩ and not NADP ϩ as cofactor. This finding is consistent with the presence of Glu-184 in the amino acid sequence of PhnY, as this residue is thought to be involved in the binding of the 2Ј-and 3Ј-hydroxyls of the adenine ribose, thereby providing cofactor specificity for NAD ϩ over NADP ϩ (34). PhnA, a PnA hydrolase from S. meliloti and a homolog of PhnA from P. fluorescens 23F (amino acid sequence identity of 56%, NCBI accession number AAC15507), belongs to the alkaline phosphatase superfamily of enzymes that includes hydrolases (e.g.…”

Section: Discussionsupporting

confidence: 84%

Genetic and Biochemical Characterization of a Pathway for the Degradation of 2-Aminoethylphosphonate in Sinorhizobium meliloti 1021

Borisova

Christman

Metcalf

et al. 2011

Journal of Biological Chemistry

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Section: Discussionsupporting

confidence: 84%

Genetic and Biochemical Characterization of a Pathway for the Degradation of 2-Aminoethylphosphonate in Sinorhizobium meliloti 1021

Borisova

Christman

Metcalf

et al. 2011

Journal of Biological Chemistry

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“…-specific ALDHs [10,47]; however, it interacts with these same hydroxyls only through an intervening water molecule in class 3 ALDH [8]. The larger distance between this residue and the adenine ribose hydroxyls, occupied by a water [3].…”

Section: Discussionmentioning

confidence: 99%

Gene Cloning and Biochemical Characterization of a NAD(P)+-Dependent Aldehyde Dehydrogenase from Bacillus licheniformis

Chen

2010

Mol Biotechnol

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A putative aldehyde dehydrogenase (ALDH) gene, ybcD (gene locus b1467), was identified in the genome sequence of Bacillus licheniformis ATCC 14580. B. licheniformis ALDH (BlALDH) encoded by ybcD consists of 488 amino acid residues with a molecular mass of approximately 52.7 kDa. The coding sequence of ybcD gene was cloned in pQE-31, and functionally expressed in recombinant Escherichia coli M15. BlALDH had a subunit molecular mass of approximately 53 kDa and the molecular mass of the native enzyme was determined to be 220 kDa by FPLC, reflecting that the oilgomeric state of this enzyme is tetrameric. The temperature and pH optima for BlALDH were 37 degrees C and 7.0, respectively. In the presence of either NAD(+) or NADP(+), the enzyme could oxidize a number of aliphatic aldehydes, particularly C3- and C5-aliphatic aldehyde. Steady-state kinetic study revealed that BlALDH had a K (M) value of 0.46 mM and a k (cat) value of 49.38/s when propionaldehyde was used as the substrate. BlALDH did not require metal ions for its enzymatic reaction, whereas the dehydrogenase activity was enhanced by the addition of disulfide reductants, 2-mercaptoethanol and dithiothreitol. Taken together, this study lays a foundation for future structure-function studies with BlALDH, a typical member of NAD(P)(+)-dependent aldehyde dehydrogenases.

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“…A homologous first Gly residue (Gly 231 ) can be found in BoxD and in all orthologs of BoxD in the database, while the second Gly residue is missing in BoxD and in its orthologs. Specificity towards either NAD ϩ or NADP ϩ seems to be largely determined by a glutamate residue that in NAD ϩ -specific ALDHs coordinates the 2Ј and 3Ј hydroxyls of the adenine ribose of NAD while potentially repelling the 2Ј phosphate of NADP ϩ (Glu 195 in ALDH2) (29). In the NADP ϩ -specific ALDHs from V. harveyi and S. mutans, a threonine (Thr 180 or Thr 175 ) instead of a glutamate residue can be found, which hydrogen bonds with its side chain to the 2Ј phosphate of NADP ϩ .…”

Section: Discussionmentioning

confidence: 99%

Aerobic Benzoyl-Coenzyme A (CoA) Catabolic Pathway in Azoarcus evansii : Conversion of Ring Cleavage Product by 3,4-Dehydroadipyl-CoA Semialdehyde Dehydrogenase

et al. 2006

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Benzoate, a strategic intermediate in aerobic aromatic metabolism, is metabolized in various bacteria via an unorthodox pathway. The intermediates of this pathway are coenzyme A (CoA) thioesters throughout, and ring cleavage is nonoxygenolytic. The fate of the ring cleavage product 3,4-dehydroadipyl-CoA semialdehyde was studied in the ␤-proteobacterium Azoarcus evansii. Cell extracts contained a benzoate-induced, NADP ؉ -specific aldehyde dehydrogenase, which oxidized this intermediate. A postulated putative long-chain aldehyde dehydrogenase gene, which might encode this new enzyme, is located on a cluster of genes encoding enzymes and a transport system required for aerobic benzoate oxidation. The gene was expressed in Escherichia coli, and the maltose-binding protein-tagged enzyme was purified and studied. It is a homodimer composed of 54 kDa (without tag) subunits and was confirmed to be the desired 3,4-dehydroadipyl-CoA semialdehyde dehydrogenase. The reaction product was identified by nuclear magnetic resonance spectroscopy as the corresponding acid 3,4-dehydroadipyl-CoA. Hence, the intermediates of aerobic benzoyl-CoA catabolic pathway recognized so far are benzoyl-CoA; 2,3-dihydro-2,3-dihydroxybenzoyl-CoA; 3,4-dehydroadipyl-CoA semialdehyde plus formate; and 3,4-dehydroadipyl-CoA. The further metabolism is thought to lead to 3-oxoadipyl-CoA, the intermediate at which the conventional and the unorthodox pathways merge.

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Coenzyme specificity in aldehyde dehydrogenase

Cited by 26 publications

References 22 publications

Genetic and Biochemical Characterization of a Pathway for the Degradation of 2-Aminoethylphosphonate in Sinorhizobium meliloti 1021

Genetic and Biochemical Characterization of a Pathway for the Degradation of 2-Aminoethylphosphonate in Sinorhizobium meliloti 1021

Gene Cloning and Biochemical Characterization of a NAD(P)+-Dependent Aldehyde Dehydrogenase from Bacillus licheniformis

Aerobic Benzoyl-Coenzyme A (CoA) Catabolic Pathway in Azoarcus evansii : Conversion of Ring Cleavage Product by 3,4-Dehydroadipyl-CoA Semialdehyde Dehydrogenase

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