Linked Life Data

11575729

Source:http://linkedlifedata.com/resource/pubmed/id/11575729

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
6
pubmed:dateCreated
2001-9-28
pubmed:databankReference
pubmed:abstractText
Beta-cyanoalanine synthase (CAS, L-3-cyanoalanine synthase; EC 4.4.1.9) is the most important enzyme in cyanide metabolism. In addition to CAS, cysteine synthase (CS, EC 4.2.99.8) possesses CAS activity. To explore the physiological significance of cyanide metabolism, we isolated the cDNA clones corresponding to purified CAS (designated PCAS-1 and PCAS-2) and CS (designated PCS-1 and PCS-2) from potato using the information of these amino acid sequences. The recombinant proteins of PCS-1, PCS-2 and PCAS-1 catalyzed both CAS and CS reactions, although the ratios between CAS and CS activity were remarkably different. PCAS-1 preferred the substrates for the CAS reaction to the substrates for the CS reaction. From the kinetic characters and homology of amino acid sequences with known CS-like proteins, PCS-1, PCS-2 and PCAS-1 were identified as cytosolic CS, plastidic CS and mitochondrial CAS, respectively. The highest level of CAS activity, CAS protein and its mRNA were detected in potato buds. Stimulation of CAS activity and protein accumulation by ethylene without the concomitant increase of its mRNA suggested that ethylene induces CAS protein accumulation at the post-transcriptional level.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Aug
pubmed:issn
0167-4412
pubmed:author
pubmed:issnType
Print
pubmed:volume
46
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
749-60
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
2001
pubmed:articleTitle
Beta-cyanoalanine synthase and cysteine synthase from potato: molecular cloning, biochemical characterization, and spatial and hormonal regulation.
pubmed:affiliation
Department of Molecular Biology and Biotechnology, Graduate School of Pharmaceutical Sciences, Chiba University, Japan.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't