Linked Life Data

17211544

Source:http://linkedlifedata.com/resource/pubmed/id/17211544

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
2007-1-12
pubmed:abstractText
Chlamydophila pneumoniae AR39 is an obligate intracellular pathogen that causes human acute and chronic respiratory tract diseases. One protein from C. pneumoniae AR39 was assigned as 4-hydroxybenzoate decarboxylase (HBDC). Assays done with the purified oxygen-sensitive protein showed that the optimum pH and temperature were 7.5 and 30 degrees C, respectively. The Km and Vmax obtained for 4-hydroxybenzoate were approximately 0.21 mM and 11.9 nM min(-1) mg(-1), respectively. During the period of 4-hydroxybenzoate decarboxylation, overall activity of the thermal-sensitive protein was 5.06 nM min(-1) mg(-1) protein. The 4-hydroxybenzoate decarboxylation was promoted by Mg(2+), Fe(2+), Mn(2+), and Ca(2+) but not by Cu(2+) or Zn(2+). The enzyme also slowly catalyzed the reverse reaction, which was phenol carboxylation.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Feb
pubmed:issn
0343-8651
pubmed:author
pubmed:issnType
Print
pubmed:volume
54
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
102-7
pubmed:meshHeading
pubmed:year
2007
pubmed:articleTitle
Purification and characterization of a 4-hydroxybenzoate decarboxylase from Chlamydophila pneumoniae AR39.
pubmed:affiliation
College of Life Sciences and Technology, Shanghai Jiaotong University, 800 Dong-Chuan Road, Shanghai, 200240, China. jianhuaLiudl@sjtu.edu.cn
pubmed:publicationType
Journal Article