Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
4
pubmed:dateCreated
1998-5-1
pubmed:databankReference
pubmed:abstractText
Degradation of long-chain alkanes by Acinetobacter sp. strain ADP1 involves rubredoxin and rubredoxin reductase. We complemented a mutant deficient in alkane utilization and sequenced four open reading frames (ORFs) on the complementing DNA. Each of these ORFs was disrupted by insertional mutagenesis on the chromosome. As determined from sequence comparisons, ORF1 and ORF4 seem to encode a rotamase of the PpiC type and an acyl coenzyme A dehydrogenase, respectively. Disruption of these ORFs does not affect alkane utilization. In contrast, the two other ORFs, alkR and alkM, are essential for growth on alkanes as sole carbon sources. alkR encodes a polypeptide with extensive homology to AraC-XyIS-like transcriptional regulators. It is located next to alkM, which encodes the terminal alkane hydroxylase, but is in the opposite orientation. Sequence homologies with other bacterial integral-membrane hydrocarbon hydroxylases suggest that AlkM may be the first member of a new protein family. The genes identified here are not linked to the rubredoxin- and rubredoxin reductase-encoding genes on the Acinetobacter sp. strain ADP1 chromosome.
pubmed:commentsCorrections
http://linkedlifedata.com/resource/pubmed/commentcorrection/9546151-1315749, http://linkedlifedata.com/resource/pubmed/commentcorrection/9546151-1999388, http://linkedlifedata.com/resource/pubmed/commentcorrection/9546151-2185139, http://linkedlifedata.com/resource/pubmed/commentcorrection/9546151-2515118, http://linkedlifedata.com/resource/pubmed/commentcorrection/9546151-3340533, http://linkedlifedata.com/resource/pubmed/commentcorrection/9546151-5781579, http://linkedlifedata.com/resource/pubmed/commentcorrection/9546151-7532480, http://linkedlifedata.com/resource/pubmed/commentcorrection/9546151-7670642, http://linkedlifedata.com/resource/pubmed/commentcorrection/9546151-7947684, http://linkedlifedata.com/resource/pubmed/commentcorrection/9546151-7948017, http://linkedlifedata.com/resource/pubmed/commentcorrection/9546151-7986042, http://linkedlifedata.com/resource/pubmed/commentcorrection/9546151-8436948, http://linkedlifedata.com/resource/pubmed/commentcorrection/9546151-8451183, http://linkedlifedata.com/resource/pubmed/commentcorrection/9546151-8516313, http://linkedlifedata.com/resource/pubmed/commentcorrection/9546151-8573125, http://linkedlifedata.com/resource/pubmed/commentcorrection/9546151-8602167, http://linkedlifedata.com/resource/pubmed/commentcorrection/9546151-8682768, http://linkedlifedata.com/resource/pubmed/commentcorrection/9546151-8930906, http://linkedlifedata.com/resource/pubmed/commentcorrection/9546151-9074511, http://linkedlifedata.com/resource/pubmed/commentcorrection/9546151-9096332, http://linkedlifedata.com/resource/pubmed/commentcorrection/9546151-9141698, http://linkedlifedata.com/resource/pubmed/commentcorrection/9546151-9150211, http://linkedlifedata.com/resource/pubmed/commentcorrection/9546151-9226277, http://linkedlifedata.com/resource/pubmed/commentcorrection/9546151-9501429
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Apr
pubmed:issn
0099-2240
pubmed:author
pubmed:issnType
Print
pubmed:volume
64
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
1175-9
pubmed:dateRevised
2009-11-18
pubmed:meshHeading
pubmed:year
1998
pubmed:articleTitle
Alkane hydroxylase from Acinetobacter sp. strain ADP1 is encoded by alkM and belongs to a new family of bacterial integral-membrane hydrocarbon hydroxylases.
pubmed:affiliation
Institut für Mikrobiologie, Biochemie und Genetik der Friedrich-Alexander-Universität Erlangen-Nürnberg, Germany.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't