TY - JOUR
T1 - Purification and characterization of aldehyde dehydrogenase with a broad substrate specificity originated from 2-phenylethanol-assimilating Brevibacterium sp. KU1309
AU - Hirano, Jun Ichiro
AU - Miyamoto, Kenji
AU - Ohta, Hiromichi
N1 - Funding Information:
Acknowledgment This research was partially supported by the Ministry of Education, Culture, Sports, Science and Technology, Grant-in-Aid for the 21st century COE Program entitled “Understanding and Control of Life’s Function via Systems Biology”, Keio University. We thank Midori Matsumoto and Hiroyuki Kawahara for N-terminal amino acid sequencing.
PY - 2007/8
Y1 - 2007/8
N2 - Phenylacetaldehyde dehydrogenase (PADH) was purified and characterized from Brevibacterium sp. KU1309, which can grow on the medium containing 2-phenylethanol as the sole carbon source. This enzyme was a homotetrameric protein with a subunit of 61 kDa. The enzyme catalyzed the oxidation of aryl (benzaldehyde, phenylacetaldehyde, 3-phenylpropionaldehyde) and aliphatic (hexanal, octanal, decanal) aldehydes to the corresponding carboxylic acids using NAD+ as the electron acceptor. The PADH activity was enhanced by several divalent cationic ions such as Mg2+, Ca2+, and Mn2+. On the other hand, it was inhibited by SH reagents (Hg 2+, p-chloromercuribenzoate, iodoacetamide, and N-ethylmaleinimide). The substrate specificity of the enzyme is compared with those of various aldehyde dehydrogenases.
AB - Phenylacetaldehyde dehydrogenase (PADH) was purified and characterized from Brevibacterium sp. KU1309, which can grow on the medium containing 2-phenylethanol as the sole carbon source. This enzyme was a homotetrameric protein with a subunit of 61 kDa. The enzyme catalyzed the oxidation of aryl (benzaldehyde, phenylacetaldehyde, 3-phenylpropionaldehyde) and aliphatic (hexanal, octanal, decanal) aldehydes to the corresponding carboxylic acids using NAD+ as the electron acceptor. The PADH activity was enhanced by several divalent cationic ions such as Mg2+, Ca2+, and Mn2+. On the other hand, it was inhibited by SH reagents (Hg 2+, p-chloromercuribenzoate, iodoacetamide, and N-ethylmaleinimide). The substrate specificity of the enzyme is compared with those of various aldehyde dehydrogenases.
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U2 - 10.1007/s00253-007-1004-y
DO - 10.1007/s00253-007-1004-y
M3 - Article
C2 - 17619188
AN - SCOPUS:34547103991
VL - 76
SP - 357
EP - 363
JO - Applied Microbiology and Biotechnology
JF - Applied Microbiology and Biotechnology
SN - 0175-7598
IS - 2
ER -