Purification and characterization of aldehyde dehydrogenase with a broad substrate specificity originated from 2-phenylethanol-assimilating Brevibacterium sp. KU1309

Jun Ichiro Hirano, Kenji Miyamoto, Hiromichi Ohta

Research output: Contribution to journalArticle

13 Citations (Scopus)

Abstract

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.

Original languageEnglish
Pages (from-to)357-363
Number of pages7
JournalApplied Microbiology and Biotechnology
Volume76
Issue number2
DOIs
Publication statusPublished - 2007 Aug

Fingerprint

Brevibacterium
Phenylethyl Alcohol
Aldehyde Dehydrogenase
Substrate Specificity
Aldehydes
Purification
Enzymes
Substrates
Chloromercuribenzoates
Iodoacetamide
Sulfhydryl Reagents
Carboxylic Acids
Carboxylic acids
NAD
Carbon
Electrons
Ions
Proteins
Oxidation
Oxidoreductases

ASJC Scopus subject areas

  • Biotechnology
  • Microbiology
  • Bioengineering
  • Microbiology (medical)

Cite this

@article{2a02b74417924362b731845ffc245931,
title = "Purification and characterization of aldehyde dehydrogenase with a broad substrate specificity originated from 2-phenylethanol-assimilating Brevibacterium sp. KU1309",
abstract = "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.",
author = "Hirano, {Jun Ichiro} and Kenji Miyamoto and Hiromichi Ohta",
year = "2007",
month = "8",
doi = "10.1007/s00253-007-1004-y",
language = "English",
volume = "76",
pages = "357--363",
journal = "Applied Microbiology and Biotechnology",
issn = "0175-7598",
publisher = "Springer Verlag",
number = "2",

}

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

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.

UR - http://www.scopus.com/inward/record.url?scp=34547103991&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=34547103991&partnerID=8YFLogxK

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 -