Purification and Characterization of Pyridoxal 4-Dehydrogenase from<i>Aureobacterium luteolum</i>

Trongpanich, Yanee; Abe, Kinuyo; Kaneda, Yasuo; Morita, Tomotake; Yagi, Toshiharu

doi:10.1271/bbb.66.543

Cited by 10 publications

(14 citation statements)

References 12 publications

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“…The reaction specificity suggests that the enzyme is a member of the aldehyde dehydrogenase family (4). However, the amino-terminal amino acid sequence of the enzyme protein showed no homology to the proteins in this family (3).…”

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confidence: 85%

“…Pyridoxal 4-dehydrogenase has been purified partially and homogeneously from Pseudomonas MA-1 (2) and Microbacterium luteolum (3), respectively. The enzyme only catalyzes the dehydrogenase (oxidation) reaction on pyridoxal, and no reverse reduction of 4-pyridoxolactone has been observed (2,3), although due to the low purity of the enzyme preparation (2) and the limited usage of the purified preparation (3), reexamination of the results is required. The reaction specificity suggests that the enzyme is a member of the aldehyde dehydrogenase family (4).…”

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confidence: 99%

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Molecular Cloning, Expression, and Properties of an Unusual Aldo-Keto Reductase Family Enzyme, Pyridoxal 4-Dehydrogenase, That Catalyzes Irreversible Oxidation of Pyridoxal

Yokochi

Yoshikane

Trongpanich

et al. 2004

Journal of Biological Chemistry

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Microbacterium luteolum YK-1 has pyridoxine degradation pathway I. We have cloned the structural gene for the second step enzyme, pyridoxal 4-dehydrogenase. The gene consists of 1,026-bp nucleotides and encodes 342 amino acids. The enzyme was overexpressed under cold shock conditions with a coexpression system and chaperonin GroEL/ES. The recombinant enzyme showed the same properties as the M. luteolum enzyme. The primary sequence of the enzyme was 54% identical with that of D-threo-aldose 1-dehydrogenase from Agrobacterium tumefaciens, a probable aldo-keto reductase (AKR). Upon multiple alignment with enzymes belonging to the 14 AKR families so far reported, pyridoxal 4-dehydrogenase was found to form a new AKR superfamily (AKR15) together with A. tumefaciens D-threo-aldose 1-dehydrogenase and Pseudomonas sp. L-fucose dehydrogenase. These enzymes belong to a distinct branch from the two main ones found in the phylogenic tree of AKR proteins. The enzymes on the new branch are characterized by their inability to reduce the corresponding lactones, which are produced from pyridoxal or sugars. Furthermore, pyridoxal 4-dehydrogenase prefers NAD ؉ to NADP ؉ as a cofactor, although AKRs generally show higher affinities for the latter.

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confidence: 85%

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confidence: 99%

Molecular Cloning, Expression, and Properties of an Unusual Aldo-Keto Reductase Family Enzyme, Pyridoxal 4-Dehydrogenase, That Catalyzes Irreversible Oxidation of Pyridoxal

Yokochi

Yoshikane

Trongpanich

et al. 2004

Journal of Biological Chemistry

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“…Compared to the values observed for AKR11C1 with the substrates listed in Table 2, human aldose reductase, B. subtilis AKR11A/B, or E. coli AKR14A1 are from 44-fold to O300-fold more active. 5,10,30 Because of the high level of sequence identity (61%) with a B. cereus D-threo-aldose 1-dehydrogenase, 19 and with the recently identified pyridoxal 4-dehydrogenase AKR15A1 (26%), 31,32 we tested whether AKR11C1 can catalyze the oxidation of pyridoxal, L-xylose and D-arabinose using NADP C as the hydride acceptor. However, no activity was detectable, suggesting that AKR11C1 does not act as a dehydrogenase.…”

Section: Substrate Specificitymentioning

confidence: 99%

“…31,32 The assay mixture (1 ml final volume) was 50 mM sodium phosphate buffer (pH 8), 1 mM NADP C , 0.1 mM AKR11C1, and 250 mM sugar substrates, or 0.5 mM pyridoxal. The rate of increase in the absorption of NADPH or 4-pyridoxolactone was followed at 25 8C by measuring absorbance at 340 and 366 nm, respectively, using a Shimadzu UV-1601 spectrophotometer.…”

Section: Model Building and Refinementmentioning

confidence: 99%

High-resolution Crystal Structure of AKR11C1 from Bacillus halodurans: An NADPH-dependent 4-Hydroxy-2,3-trans-nonenal Reductase

Marquardt

Kostrewa

Rajkumar

et al. 2005

Journal of Molecular Biology

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“…4) The primary structure of the enzyme was determined based on cloning and expression of its gene in Escherichia coli. The gene encoding PN 4-oxidase was found on a chromosomal DNA.…”

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Purification, Molecular Cloning, and Characterization of Pyridoxine 4-Oxidase fromMicrobacterium luteolum

Kaneda

Ohnishi

Yagi

2002

Bioscience, Biotechnology, and Biochemistry

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Pyridoxine 4-oxidase (EC 1.1.3.12, PN 4-oxidase), which catalyzes the oxidation of PN by oxygen or other hydrogen acceptors to form pyridoxal and hydrogen peroxide or reduced forms of the acceptors, respectively, was purified for the first time to homogeneity from Microbacterium luteolum YK-1 (=Aureobacterium luteolum YK-1). The purified enzyme required FAD for its catalytic activity and stability. The enzyme was a monomeric protein with the subunit molecular mass of 53,000 +/- 1,000 Da. PN was the only substrate as the hydrogen donor. Oxygen, 2,6-dichloroindophenol, and vitamin K3 were good substrates as the hydrogen acceptor. The gene (pno) encoding PN 4-oxidase was cloned. The gene encodes a protein of 507 amino acid residues corresponding to the molecular mass of the subunit. PN 4-oxidase was expressed in Escherichia coli and found to have the same properties as the native enzyme from M. luteolum YK-1. Comparisons of primary and secondary structures with other proteins showed that the enzyme belongs to the GMC oxidoreductase family. M. luteolum YK-1 has four plasmids. The pno gene was found on a chromosomal DNA. Search for genes similar in sequence in other organisms suggested that a nitrogen-fixing symbiotic bacterium, Mesorhizobium loti, which harbors two plasmids, has a PN degradation pathway I in chromosomal DNA.

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Purification and Characterization of Pyridoxal 4-Dehydrogenase fromAureobacterium luteolum

Cited by 10 publications

References 12 publications

Molecular Cloning, Expression, and Properties of an Unusual Aldo-Keto Reductase Family Enzyme, Pyridoxal 4-Dehydrogenase, That Catalyzes Irreversible Oxidation of Pyridoxal

Molecular Cloning, Expression, and Properties of an Unusual Aldo-Keto Reductase Family Enzyme, Pyridoxal 4-Dehydrogenase, That Catalyzes Irreversible Oxidation of Pyridoxal

High-resolution Crystal Structure of AKR11C1 from Bacillus halodurans: An NADPH-dependent 4-Hydroxy-2,3-trans-nonenal Reductase

Purification, Molecular Cloning, and Characterization of Pyridoxine 4-Oxidase fromMicrobacterium luteolum

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