The enzyme, characterized from the bacterium Escherichia coli, is involved in a putrescine catabolic pathway. It has a broad substrate range, and can also catalyse the activities of EC 1.2.1.19, aminobutyraldehyde dehydrogenase, and EC 1.2.1.24, succinate-semialdehyde dehydrogenase (NAD+).
The enzyme appears in viruses and cellular organisms
The enzyme, characterized from the bacterium Escherichia coli, is involved in a putrescine catabolic pathway. It has a broad substrate range, and can also catalyse the activities of EC 1.2.1.19, aminobutyraldehyde dehydrogenase, and EC 1.2.1.24, succinate-semialdehyde dehydrogenase (NAD+).
Substrates: activity is decreased by 73% when NAD+ is replaced with NADP+. The reduction of 3-hydroxypropionate to 3-hydroxypropionaldehyde is not catalyzed with NADPH as cofactor Products: -
Substrates: activity for the reduction of 3-hydroxypropionate to 3-hydroxypropionaldehyde is only 4% of that for the corresponding oxidation reaction, indicating that this enzyme catalyzes oxidation reactions under most physiological conditions Products: -
Substrates: 3-hydroxypropionaldehyde i.e. 3-HPA, 3-hydroxypropionic acid i.e. 3-HP, PuuC overexpression enhances the glycerol carbon flux towards 3-hydroxypropionaldehyde Products: -
Substrates: development and evaluation recombinant Klebsiella pneumoniae, for the production of 3-hydroxypropionic acid from glycerol, therefor PuuC together with a coenzyme B12-dependent glycerol dehydratase are overexpressed while two major oxidoreductases, DhaT and YqhD, are disrupted eliminating the production of 1,3-propanediol out of 3-hydroxypropionaldehyde Products: -
utilizes both NAD+ and NADP+ as cofactors, NAD+ is the preferred cofactor for all substrates except benzaldehyde and 2-furaldehyde. In case of 3-hydroxypropionaldehyde, the activity is decreased by 73% when NAD+ is replaced with NADP+
utilizes both NAD+ and NADP+ as cofactors, NAD+ is the preferred cofactor for all substrates except benzaldehyde and 2-furaldehyde. In case of 3-hydroxypropionaldehyde, the activity is decreased by 73% when NAD+ is replaced with NADP+
PuuC is a nonspecific aldehyde dehydrogenase that oxidizes all the aldehydes in putrescine catabolism. Strains lacking PuuC activity have a doubling time 50% greater than the wild type with putrescine as the sole nitrogen source. Strains with deletions of putrescine aminotransferase PatA and any of PuuA, PuuB, or PuuC do not grow with putrescine as the nitrogen source
PuuC of Klebsiella pneumoniae alone or with coenzyme B12-dependent glycerol dehydratase, DhaB overexpressed homologously, and two major oxidoreductases, DhaT and YqhD, disrupted resulting in KpC_DELTA_dhaT_DELTA_yqhD strain and KpBC_DELTA_dhaT_DELTA_yqhD strain, overexpressing the glycerol dehydratase DhaB, too
the recombinant strain SH254 producing 3-hydroxypropionate from glycerol is developed by cloning of dhaB and aldH genes in Escherichia coli BL21 under different regulatory promoters
3-hydroxypropionic acid is an important compound from which several commodity and specialty chemicals can be generated. The DELTAdhaT mutant (deletion in gene dhaT, encoding NADH-dependent 1,3-propanediol oxidoreductase) overexpressing PuuC has a potential to coproduce two commercially valuable products, 3-hydroxypropionic acid and 1,3-propanediol
3-hydroxypropionic acid is an important compound from which several commodity and specialty chemicals can be generated. The recombinant strain SH254 producing 3-hydroxypropionate from glycerol is developed by cloning of dhaB and aldH genes in Escherichia coli BL21 under different regulatory promoters. The recombinant SH254 can accumulate 3-hydroxypropionic acid from glycerol at 6.5 mmol/l in 30 h
3-hydroxypropionic acid is an important platform chemical that can be used to synthesize a range of chemical compounds, such as acrylic acid, 1,3-propanediol, methyl acrylate, malonic acid, acrylamide, and hydroxyamides
3-hydroxypropionic acid is an important compound from which several commodity and specialty chemicals can be generated. The DELTAdhaT mutant (deletion in gene dhaT, encoding NADH-dependent 1,3-propanediol oxidoreductase) overexpressing PuuC has a potential to coproduce two commercially valuable products, 3-hydroxypropionic acid and 1,3-propanediol
Jo, J.E.; Mohan Raj, S.; Rathnasingh, C.; Selvakumar, E.; Jung, W.C.; Park, S.
Cloning, expression, and characterization of an aldehyde dehydrogenase from Escherichia coli K-12 that utilizes 3-hydroxypropionaldehyde as a substrate
Raj, S.; Rathnasingh, C.; Jung, W.; Selvakumar, E.; Park, S.
A novel NAD+-dependent aldehyde dehydrogenase encoded by the puuC gene of Klebsiella pneumoniae DSM 2026 that utilizes 3-hydroxypropionaldehyde as a substrate