Linked Life Data

15208336

Source:http://linkedlifedata.com/resource/pubmed/id/15208336

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
404
pubmed:dateCreated
2004-8-9
pubmed:abstractText
The sulphate assimilation pathway provides reduced sulphur for the synthesis of the amino acids cysteine and methionine. These are the essential building blocks of proteins and further sources of reduced sulphur for the synthesis of coenzymes and various secondary compounds. Several recent reports identified the adenosine 5'-phosphosulphate reductase (APR) as the enzyme with the greatest control over the pathway. In this review, a short historical excursion into the investigations of sulphate assimilation is given with emphasis on the proposed alternative pathways to APR, via 'bound sulphite' or via PAPS reductase. The evolutionary past of APR is reviewed, based on phylogenetic analysis of APR and PAPS reductase sequences. Furthermore, recent biochemical analyses of APR that identified an iron-sulphur centre as a cofactor, proposed functions for different protein domains, and addressed the enzyme mechanism are summarized. Finally, questions that have to be addressed in order to improve understanding of the molecular mechanism and regulation of APR have been identified.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Aug
pubmed:issn
0022-0957
pubmed:author
pubmed:issnType
Print
pubmed:volume
55
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
1775-83
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
2004
pubmed:articleTitle
Plant adenosine 5'-phosphosulphate reductase: the past, the present, and the future.
pubmed:affiliation
Albert-Ludwigs-University of Freiburg, Institute of Forest Botany and Tree Physiology, Georges-Köhler-Allee 053, D-79110 Freiburg, Germany. Stanislav.Kopriva@ctp.uni-freiburg.de
pubmed:publicationType
Journal Article, Review