Linked Life Data

10531498

Source:http://linkedlifedata.com/resource/pubmed/id/10531498

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
Pt 11
pubmed:dateCreated
2000-1-27
pubmed:abstractText
Guanidinoacetate methyltransferase is the enzyme which catalyzes the last step of creatine biosynthesis. The enzyme is found ubiquitously and in abundance in the livers of all vertebrates. Recombinant rat-liver guanidinoacetate methyltransferase has been crystallized with guanidinoacetate and S-adenosylhomocysteine. The crystals belong to the monoclinic space group P2(1), with unit-cell parameters a = 54.8, b = 162.5, c = 56.1 A, beta = 96.8 (1) degrees at 93 K, and typically diffract beyond 2.8 A.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Nov
pubmed:issn
0907-4449
pubmed:author
pubmed:issnType
Print
pubmed:volume
55
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
1928-9
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed:year
1999
pubmed:articleTitle
Crystallization and preliminary x-ray diffraction studies of guanidinoacetate methyltransferase from rat liver.
pubmed:affiliation
Department of Molecular Biosciences, University of Kansas, Lawrence, KS 66045-0045, USA.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S.