Linked Life Data

21154803

Source:http://linkedlifedata.com/resource/pubmed/id/21154803

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1
pubmed:dateCreated
2010-12-30
pubmed:abstractText
CYP101C1 from Novosphingobium aromaticivorans DSM12444 is a homologue of CYP101D1 and CYP101D2 enzymes from the same bacterium and CYP101A1 from Pseudomonas putida. CYP101C1 does not bind camphor but is capable of binding and hydroxylating ionone derivatives including ?- and ?-ionone and ?-damascone. The activity of CYP101C1 was highest with ?-damascone (k(cat)=86 s(-1)) but ?-ionone oxidation was the most regioselective (98?% at C3). The crystal structures of hexane-2,5-diol- and ?-ionone-bound CYP101C1 have been solved; both have open conformations and the hexanediol-bound form has a clear access channel from the heme to the bulk solvent. The entrance of this channel is blocked when ?-ionone binds to the enzyme. The heme moiety of CYP101C1 is in a significantly different environment compared to the other structurally characterised CYP101 enzymes. The likely ferredoxin binding site on the proximal face of CYP101C1 has a different topology but a similar overall positive charge compared to CYP101D1 and CYP101D2, all of which accept electrons from the ArR/Arx class I electron transfer system.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jan
pubmed:issn
1439-7633
pubmed:author
pubmed:issnType
Electronic
pubmed:day
3
pubmed:volume
12
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
88-99
pubmed:meshHeading
pubmed:year
2011
pubmed:articleTitle
Structural Analysis of CYP101C1 from Novosphingobium aromaticivorans DSM12444.
pubmed:affiliation
National Laboratory of Macromolecules, Institute of Biophysics, Chinese Academy of Science, Beijing 100101, China.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't