Linked Life Data

8756596

Source:http://linkedlifedata.com/resource/pubmed/id/8756596

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
1996-9-27
pubmed:databankReference
pubmed:abstractText
Allene oxide synthase, an enzyme of the octadecanoid pathway to jasmonates, was cloned from Arabidopsis thaliana as a full-length cDNA encoding a polypeptide of 517 amino acids with a calculated molecular mass of 58705 Da. From the sequence, an N-terminal transit peptide of 21 amino acids resembling chloroplast transit peptides was deduced. Three out of four invariant amino acid residues of cytochrome P450 heme-binding domains are conserved and properly positioned in the enzyme coding region, including the heme-accepting cysteine (Cys-470). Southern analysis indicated in A. thaliana only one allene oxide synthase gene to be present. While transcript levels were rapidly and transiently induced after wounding of the leaves, allene oxide synthase activity remained nearly constant at a low level of ca. 0.8 nkat per mg of protein. The cDNA encoding A. thaliana allene oxide synthase was highly expressed in bacteria giving rise to a polypeptide of the calculated molecular mass. The protein was enzymatically active, and verification of the reaction products by GC-MS showed that it was capable of utilizing not only 13-hydroperoxylinolenic acid (13-hydroperoxy-9(Z), 11(E), 15(Z)-octadecatrienoic acid), but also 13-hydroperoxylinoleic acid (13-hydroperoxy-9(Z), 11(E)-octadecadienoic acid) as substrate. The data suggest parallel pathways to jasmonates from linolenic acid or linoleic acid in A. thaliana.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
May
pubmed:issn
0167-4412
pubmed:author
pubmed:issnType
Print
pubmed:volume
31
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
323-35
pubmed:dateRevised
2007-11-15
pubmed:meshHeading
pubmed-meshheading:8756596-Amino Acid Sequence, pubmed-meshheading:8756596-Arabidopsis, pubmed-meshheading:8756596-Base Sequence, pubmed-meshheading:8756596-Cloning, Molecular, pubmed-meshheading:8756596-Cyclopentanes, pubmed-meshheading:8756596-DNA, Complementary, pubmed-meshheading:8756596-DNA Primers, pubmed-meshheading:8756596-Genes, Plant, pubmed-meshheading:8756596-Intramolecular Oxidoreductases, pubmed-meshheading:8756596-Isomerases, pubmed-meshheading:8756596-Mass Spectrometry, pubmed-meshheading:8756596-Molecular Sequence Data, pubmed-meshheading:8756596-Oxylipins, pubmed-meshheading:8756596-RNA, Messenger, pubmed-meshheading:8756596-RNA, Plant, pubmed-meshheading:8756596-Recombinant Proteins, pubmed-meshheading:8756596-Sequence Alignment, pubmed-meshheading:8756596-Sequence Homology, Amino Acid
pubmed:year
1996
pubmed:articleTitle
Cloning, molecular and functional characterization of Arabidopsis thaliana allene oxide synthase (CYP 74), the first enzyme of the octadecanoid pathway to jasmonates.
pubmed:affiliation
Lehrstuhl für Pflanzenphysiologie, Ruhr-Universität Bochum, Germany.
pubmed:publicationType
Journal Article, Comparative Study, Research Support, Non-U.S. Gov't