Linked Life Data

18417078

Source:http://linkedlifedata.com/resource/pubmed/id/18417078

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1
pubmed:dateCreated
2008-5-9
pubmed:abstractText
The gene encoding m-hydroxybenzoate hydroxylase (mobA) was cloned from Comamonas testosteroni GZ39. MobA converts m-hydroxybenzoate and to a lesser extent p-hydroxybenzoate to protocatechuate. To explore the structural and functional relationships in phenolic acid monooxygenases, MobA was subjected to in vitro mutagenesis by error-prone PCR and the mutant MobAs were screened for their ability to oxidize phenol or 3-aminophenol. A mutant MobA with a single V257A substitution was able to transform phenol to catechol, providing the first example of monooxygenase acting on phenolic acids that can also hydroxylate phenol. The mutant MobA also has enhanced ability to transform resorcinol, hydroquinone, p-hydroxybenzoate, 2,5-dihydroxybenzoate, 3,4-dihydroxybenzoate, 3-chlorophenol, 4-chlorophenol, 4-chlororesorcinol, and 4-nitrophenol. Several MobA mutants were obtained for their ability to transform 3-aminophenol to a related substituted catechol. Mutant MobAs with single amino acid substitutions (H135P, A400G, or D416A) were derived from these mutants and verified for their ability to transform 3-aminophenol.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jun
pubmed:issn
1090-2104
pubmed:author
pubmed:issnType
Electronic
pubmed:day
20
pubmed:volume
371
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
149-53
pubmed:meshHeading
pubmed:year
2008
pubmed:articleTitle
Examination and expansion of the substrate range of m-hydroxybenzoate hydroxylase.
pubmed:affiliation
Biotechnology Center for Agriculture and the Environment, School of Environmental and Biological Sciences, Rutgers University, 59 Dudley Road, New Brunswick, NJ 08901-8520, USA. hkchang@rci.rutgers.edu
pubmed:publicationType
Journal Article