Switch to
Predicate | Object |
---|---|
rdf:type | |
lifeskim:mentions | |
pubmed:issue |
24
|
pubmed:dateCreated |
1997-7-14
|
pubmed:databankReference | |
pubmed:abstractText |
Primary structural information of a plant aldehyde oxidase (AO), which was purified from maize coleoptiles using indole-3-acetaldehyde as a substrate, was obtained by sequencing a series of cleavage peptides, permitting the cloning of the corresponding cDNA (zmAO-1). The complete nucleotide sequence was determined; the deduced amino acid sequence encodes a protein of 1358 amino acid residues of Mr 146,681, which is consistent with the size of the AO monomeric subunit. There is a significant similarity with AO from mammals and xanthine dehydrogenases from various sources. The maize AO polypeptide contains consensus sequences for iron-sulfur centers and a putative molybdopterin cofactor-binding domain. In addition, another cDNA (zmAO-2), highly homologous to zmAO-1 at both the nucleotide and amino acid sequence levels, was cloned. zmAO-2 would encode a protein of 1349 amino acid residues of Mr 145,173 and has molecular characteristics similar to those of zmAO-1. zmAO-1 was expressed at a high level in roots, which was closely correlated with immunoblotting results using antiserum raised against the purified maize AO protein, whereas zmAO-2 was expressed at a higher level in coleoptiles than in roots. We propose each zmAO may have a unique function during plant development.
|
pubmed:language |
eng
|
pubmed:journal | |
pubmed:citationSubset |
IM
|
pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Aldehyde Oxidase,
http://linkedlifedata.com/resource/pubmed/chemical/Aldehyde Oxidoreductases,
http://linkedlifedata.com/resource/pubmed/chemical/DNA, Complementary,
http://linkedlifedata.com/resource/pubmed/chemical/DNA Probes,
http://linkedlifedata.com/resource/pubmed/chemical/Immune Sera
|
pubmed:status |
MEDLINE
|
pubmed:month |
Jun
|
pubmed:issn |
0021-9258
|
pubmed:author | |
pubmed:issnType |
Print
|
pubmed:day |
13
|
pubmed:volume |
272
|
pubmed:owner |
NLM
|
pubmed:authorsComplete |
Y
|
pubmed:pagination |
15280-5
|
pubmed:dateRevised |
2006-11-15
|
pubmed:meshHeading |
pubmed-meshheading:9182554-Aldehyde Oxidase,
pubmed-meshheading:9182554-Aldehyde Oxidoreductases,
pubmed-meshheading:9182554-Amino Acid Sequence,
pubmed-meshheading:9182554-Base Sequence,
pubmed-meshheading:9182554-Cloning, Molecular,
pubmed-meshheading:9182554-DNA, Complementary,
pubmed-meshheading:9182554-DNA Probes,
pubmed-meshheading:9182554-Hydrolysis,
pubmed-meshheading:9182554-Immune Sera,
pubmed-meshheading:9182554-Immunoblotting,
pubmed-meshheading:9182554-Molecular Sequence Data,
pubmed-meshheading:9182554-Plants,
pubmed-meshheading:9182554-Sequence Homology, Amino Acid
|
pubmed:year |
1997
|
pubmed:articleTitle |
Cloning and molecular characterization of plant aldehyde oxidase.
|
pubmed:affiliation |
Frontier Research Program, Wako-shi, Saitama, Japan.
|
pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
|