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+).
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The taxonomic range for the selected organisms is: Escherichia coli The enzyme appears in selected 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+).
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
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
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
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 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
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