Linked Life Data

24171

Source:http://linkedlifedata.com/resource/pubmed/id/24171

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2-3
pubmed:dateCreated
1978-4-17
pubmed:abstractText
3-Hydroxykynureninase was purified from rat liver. The Michaelis constants for L-kynurenine and L-3-hydroxykynurenine were determined to be 2.33 X 10(-4)M and 6.85 X 10(-5)M, respectively, at pH 8.41 and 37 degrees. With L-kynurenine as substrate, the enzyme was competitively inhibited by L-alanine, 3-hydroxyanthranilic acid, and several other compounds which contained structural features of either amino acid or aryl portions of the substrate. The effect of pH on the initial velocity, maximal velocity, and Michaelis constant, using L-kynurenine as substrate, was studied. Maximal velocity was strongly pH-dependent, with a maximum at pH 8.4. The Michaelis constant decreased from 11.4 X 10(-4)M at pH 7.1 to 1.30 X 10(-4)M at pH 9.0. Logarithmic plots of these data showed pKa's for functional groups ionizing in the enzyme-substrate complex and free enzyme active center of 7.6 and 8.5, respectively. Possible groups responsible for these ionizations were discussed.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Dec
pubmed:issn
0300-8177
pubmed:author
pubmed:issnType
Print
pubmed:day
29
pubmed:volume
18
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
71-5
pubmed:dateRevised
2008-11-21
pubmed:meshHeading
pubmed:year
1977
pubmed:articleTitle
Kinetic studies on 3-hydroxykynureninase from rat liver.
pubmed:publicationType
Journal Article, In Vitro