Linked Life Data

6697989

Source:http://linkedlifedata.com/resource/pubmed/id/6697989

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
1984-4-11
pubmed:abstractText
Pyridoxine-5-phosphate oxidase has been purified 2250-fold from pig brain by affinity chromatography. The enzyme of 60000 molecular weight is made up of two identical size subunits and binds 1 mol of FMN/mol dimer. 1 mol of the fluorescent inhibitor phospho-pyridoxal oxime interacts with 1 mol of the dimeric protein to yield a dissociation constant KD = 0.2 microM. Resolution of the holoenzyme into apoprotein and free FMN does not induce dissociation of the dimeric structure. The oxidase catalyzes the oxidation of the natural substrates pyridoxine 5-phosphate and pyridoxamine 5-phosphate, but phospho-pyridoxyl derivatives of the aromatic carboxylic acids, p-aminobenzoate and m-aminobenzoate, are also excellent substrates of the enzyme. Introduction of electron-withdrawing substituents into the structure of benzene increases the kcat values. A comparison of the kcat values obtained with several synthetic substrates suggests that electron-withdrawing substituents tend to stabilize carbanionic intermediates formed in the earlier stages of catalysis.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jan
pubmed:issn
0014-2956
pubmed:author
pubmed:issnType
Print
pubmed:day
16
pubmed:volume
138
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
327-32
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed:year
1984
pubmed:articleTitle
Brain pyridoxine-5-phosphate oxidase. A dimeric enzyme containing one FMN site.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S.