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Thermostable NADP(+)-dependent medium-chain alcohol dehydrogenase from Acinetobacter sp. strain M-1: purification and characterization and gene expression in Escherichia coli.
Appl Environ Microbiol. 2000 Dec; 66(12):5231-5.AE

Abstract

NADPH-dependent alkylaldehyde reducing enzyme, which was greatly induced by n-hexadecane, from Acinetobacter sp. strain M-1 was purified and characterized. The purified enzyme had molecular masses of 40 kDa as determined by sodium dodecyl sulfate-polyacrylamide gel electrophoresis and 160 kDa as determined by gel filtration chromatography. The enzyme, which was shown to be highly thermostable, was most active toward n-heptanal and could use n-alkylaldehydes ranging from C(2) to C(14) and several substituted benzaldehydes, including the industrially important compounds cinnamyl aldehyde and anisaldehyde, as substrates. The alrA gene coding for this enzyme was cloned, and its nucleotide sequence was determined. The deduced amino acid sequence encoded by the alrA gene exhibited homology to the amino acid sequences of zinc-containing alcohol dehydrogenases from various sources. The gene could be highly expressed in Escherichia coli, and the product was purified to homogeneity by simpler procedures from the recombinant than from the original host. Our results show that this enzyme can be used for industrial bioconversion of useful alcohols and aldehydes.

Authors+Show Affiliations

Division of Applied Life Sciences, Graduate School of Agriculture, Kyoto University, Kitashirakawa-Oiwake, Sakyo-ku, Kyoto 606-8502, Japan.No affiliation info availableNo affiliation info availableNo affiliation info available

Pub Type(s)

Journal Article

Language

eng

PubMed ID

11097895

Citation

Tani, A, et al. "Thermostable NADP(+)-dependent Medium-chain Alcohol Dehydrogenase From Acinetobacter Sp. Strain M-1: Purification and Characterization and Gene Expression in Escherichia Coli." Applied and Environmental Microbiology, vol. 66, no. 12, 2000, pp. 5231-5.
Tani A, Sakai Y, Ishige T, et al. Thermostable NADP(+)-dependent medium-chain alcohol dehydrogenase from Acinetobacter sp. strain M-1: purification and characterization and gene expression in Escherichia coli. Appl Environ Microbiol. 2000;66(12):5231-5.
Tani, A., Sakai, Y., Ishige, T., & Kato, N. (2000). Thermostable NADP(+)-dependent medium-chain alcohol dehydrogenase from Acinetobacter sp. strain M-1: purification and characterization and gene expression in Escherichia coli. Applied and Environmental Microbiology, 66(12), 5231-5.
Tani A, et al. Thermostable NADP(+)-dependent Medium-chain Alcohol Dehydrogenase From Acinetobacter Sp. Strain M-1: Purification and Characterization and Gene Expression in Escherichia Coli. Appl Environ Microbiol. 2000;66(12):5231-5. PubMed PMID: 11097895.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Thermostable NADP(+)-dependent medium-chain alcohol dehydrogenase from Acinetobacter sp. strain M-1: purification and characterization and gene expression in Escherichia coli. AU - Tani,A, AU - Sakai,Y, AU - Ishige,T, AU - Kato,N, PY - 2000/12/1/pubmed PY - 2001/3/3/medline PY - 2000/12/1/entrez SP - 5231 EP - 5 JF - Applied and environmental microbiology JO - Appl. Environ. Microbiol. VL - 66 IS - 12 N2 - NADPH-dependent alkylaldehyde reducing enzyme, which was greatly induced by n-hexadecane, from Acinetobacter sp. strain M-1 was purified and characterized. The purified enzyme had molecular masses of 40 kDa as determined by sodium dodecyl sulfate-polyacrylamide gel electrophoresis and 160 kDa as determined by gel filtration chromatography. The enzyme, which was shown to be highly thermostable, was most active toward n-heptanal and could use n-alkylaldehydes ranging from C(2) to C(14) and several substituted benzaldehydes, including the industrially important compounds cinnamyl aldehyde and anisaldehyde, as substrates. The alrA gene coding for this enzyme was cloned, and its nucleotide sequence was determined. The deduced amino acid sequence encoded by the alrA gene exhibited homology to the amino acid sequences of zinc-containing alcohol dehydrogenases from various sources. The gene could be highly expressed in Escherichia coli, and the product was purified to homogeneity by simpler procedures from the recombinant than from the original host. Our results show that this enzyme can be used for industrial bioconversion of useful alcohols and aldehydes. SN - 0099-2240 UR - https://www.unboundmedicine.com/medline/citation/11097895/Thermostable_NADP_+__dependent_medium_chain_alcohol_dehydrogenase_from_Acinetobacter_sp__strain_M_1:_purification_and_characterization_and_gene_expression_in_Escherichia_coli_ L2 - http://aem.asm.org/cgi/pmidlookup?view=long&pmid=11097895 DB - PRIME DP - Unbound Medicine ER -