Disease relevance of yghZ

• A novel aldo-keto reductase from Escherichia coli can increase resistance to methylglyoxal toxicity [1].
• 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) [2].
• 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 [2].
• A new member of the aldo-keto reductase family from the plant pathogen Xylella fastidiosa [3].

High impact information on yghZ

• The recently identified AKR7A2 was shown to differ from the AKR1 isoenzymes in being able to catalyse the reduction of 2-carboxybenzaldehyde [4].
• The activity was identified to an open reading frame we call tas, the sequence for which has homology with a variety of known genes with aldo-keto reductase activity [5].
• This is the first instance where point mutations in the conserved catalytic tetrad of an AKR yielded enzymes which were still catalytically active [6].
• Aldose reductase is a NADPH-dependent aldo-keto reductase involved in the pathogenesis of some diabetic and galactosemic complications [7].
• The temporal pattern of expression of this aldo-keto reductase gene was delineated by extracting ovarian RNA at 0, 2, 4, 8, 12, and 24 h after induction of ovulation via injection of the primed animals with hCG [8].

Biological context of yghZ

• Two cDNAs encoding leaf-specific AKR proteins (DpAR1 and DpAR2) were isolated from a D. purpurea cDNA library using the rat Delta4-3-ketosteroid 5beta-reductase clone [9].
• The deduced amino acid sequences of the two enzymes showed high similarity to each other and to several proteins of the aldo-keto reductase (AKR) superfamily [10].

Associations of yghZ with chemical compounds

• Molecular cloning, expression, and properties of an unusual aldo-keto reductase family enzyme, pyridoxal 4-dehydrogenase, that catalyzes irreversible oxidation of pyridoxal [2].
• Purification and characterization of NADPH-dependent aldo-keto reductase specific for beta-keto esters from Penicillium citrinum, and production of methyl (S)-4-bromo-3-hydroxybutyrate [11].

References