The flavoprotein isobutylamine N-hydroxylase (IBAH) catalyzes the
oxidation of isobutylamine to isobutylhydroxylamine, a key step
in the biosynthesis of the azoxy antibiotic valanimycin. By using
oligonucleotide primers designed from peptide sequence information
derived from native IBAH, a fragment of the gene (vlmH) encoding
IBAH was amplified by PCR from a genomic library of the valanimycin-producing
organism, Streptomyces viridifaciens MG456-hF10. The gene fragment
was then employed as a probe to clone the entire vlmH gene from
an S. viridifaciens genomic library. Overexpression of the vlmH
gene in Escherichia coli gave a soluble protein that was purified
to homogeneity. The purified protein exhibited the catalytic activity
expected for IBAH. The deduced amino acid sequence of IBAH exhibited
the greatest similarity to the Sox/DszC protein from Rhodococcus
sp. strain IGT38, a flavoprotein involved in the oxidation of dibenzothiophene
to the corresponding sulfone. Significant similarities were also
found between the amino acid sequence of IBAH and those of the acyl
coenzyme A dehydrogenases.
%0 Journal Article
%1 citeulike:708308
%A Parry, R. J.
%A Li, W.
%A Cooper, H. N.
%C Department of Chemistry, Rice University, Houston, Texas 77251, USA.
parry@rice.edu
%D 1997
%J J Bacteriol
%K n-oxidation biosynthesis
%N 2
%P 409--416
%T Cloning, analysis, and overexpression of the gene encoding isobutylamine
N-hydroxylase from the valanimycin producer, Streptomyces viridifaciens.
%U http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&dopt=Abstract&list_uids=8990292
%V 179
%X The flavoprotein isobutylamine N-hydroxylase (IBAH) catalyzes the
oxidation of isobutylamine to isobutylhydroxylamine, a key step
in the biosynthesis of the azoxy antibiotic valanimycin. By using
oligonucleotide primers designed from peptide sequence information
derived from native IBAH, a fragment of the gene (vlmH) encoding
IBAH was amplified by PCR from a genomic library of the valanimycin-producing
organism, Streptomyces viridifaciens MG456-hF10. The gene fragment
was then employed as a probe to clone the entire vlmH gene from
an S. viridifaciens genomic library. Overexpression of the vlmH
gene in Escherichia coli gave a soluble protein that was purified
to homogeneity. The purified protein exhibited the catalytic activity
expected for IBAH. The deduced amino acid sequence of IBAH exhibited
the greatest similarity to the Sox/DszC protein from Rhodococcus
sp. strain IGT38, a flavoprotein involved in the oxidation of dibenzothiophene
to the corresponding sulfone. Significant similarities were also
found between the amino acid sequence of IBAH and those of the acyl
coenzyme A dehydrogenases.
@article{citeulike:708308,
abstract = {The flavoprotein isobutylamine N-hydroxylase (IBAH) catalyzes the
oxidation of isobutylamine to isobutylhydroxylamine, a key step
in the biosynthesis of the azoxy antibiotic valanimycin. By using
oligonucleotide primers designed from peptide sequence information
derived from native IBAH, a fragment of the gene (vlmH) encoding
IBAH was amplified by PCR from a genomic library of the valanimycin-producing
organism, Streptomyces viridifaciens MG456-hF10. The gene fragment
was then employed as a probe to clone the entire vlmH gene from
an S. viridifaciens genomic library. Overexpression of the vlmH
gene in Escherichia coli gave a soluble protein that was purified
to homogeneity. The purified protein exhibited the catalytic activity
expected for IBAH. The deduced amino acid sequence of IBAH exhibited
the greatest similarity to the Sox/DszC protein from Rhodococcus
sp. strain IGT38, a flavoprotein involved in the oxidation of dibenzothiophene
to the corresponding sulfone. Significant similarities were also
found between the amino acid sequence of IBAH and those of the acyl
coenzyme A dehydrogenases.},
added-at = {2007-02-02T11:54:15.000+0100},
address = {Department of Chemistry, Rice University, Houston, Texas 77251, USA.
parry@rice.edu},
author = {Parry, R. J. and Li, W. and Cooper, H. N.},
biburl = {https://www.bibsonomy.org/bibtex/2e2ec4547412753b5d9d4dc2849992a71/robert},
citeulike-article-id = {708308},
interhash = {4f6f3b74cab5b00aaed251b0f7cc7483},
intrahash = {e2ec4547412753b5d9d4dc2849992a71},
issn = {0021-9193},
journal = {J Bacteriol},
keywords = {n-oxidation biosynthesis},
month = {January},
number = 2,
pages = {409--416},
priority = {2},
timestamp = {2007-02-02T11:54:15.000+0100},
title = {Cloning, analysis, and overexpression of the gene encoding isobutylamine
N-hydroxylase from the valanimycin producer, Streptomyces viridifaciens.},
url = {http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve\&db=pubmed\&dopt=Abstract\&list_uids=8990292},
volume = 179,
year = 1997
}