Linked Life Data

19874134

Source:http://linkedlifedata.com/resource/pubmed/id/19874134

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
3
pubmed:dateCreated
2010-4-21
pubmed:abstractText
N-Acetylgalactosamine kinase (GALK2) is a small molecule kinase from the GHMP family which phosphorylates N-acetylgalactosamine at the expense of ATP. Recombinant GALK2 expressed in, and purified from, Escherichia coli was shown to be active with the following kinetic parameters: Michaelis constant for ATP, 14 +/- 3 microM; Michaelis constant for N-acetylgalactosamine, 40 +/- 14 microM; and turnover number, 1.0 +/- 0.1 s(-1). The combination of substrate inhibition by N-acetylgalactosamine and alpha-methylgalactopyranoside acting as an uncompetitive inhibitor with respect to ATP suggested that the enzyme has an ordered ternary complex mechanism in which ATP is the first substrate to bind. The effects of pH on the kinetic parameters provided evidence for ionizable residues playing a role in substrate binding and catalysis. These results are discussed in the context of the mechanisms of the GHMP kinases.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jun
pubmed:issn
1475-6374
pubmed:author
pubmed:issnType
Electronic
pubmed:volume
25
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
370-6
pubmed:meshHeading
pubmed:year
2010
pubmed:articleTitle
Mechanistic studies on human N-acetylgalactosamine kinase.
pubmed:affiliation
Queen's University Belfast, Belfast, United Kingdom.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't