A spinach cDNA with homology to S-adenosylmethionine decarboxylase

S-Adenosylmethionine decarboxylase is an important enzyme in polyamine biosynthesis. It catalyzes the decarboxylation of S-adenosylmethionine, which serves as an aminopropyl donor for the conversion of putrescine to spermidine. A common feature of S-adenosylmethionine decarboxylases is that it is sy...

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Bibliographic Details
Published in:Plant physiology (Bethesda) 1995-04, Vol.107 (4), p.1461-1462
Main Authors: Bolle, C. (Ludwig-Maximilians-Universitat, Munchen, Germany.), Herrmann, R.G, Oelmuller, R
Format: Article
Language:English
Subjects:
Adenosylmethionine Decarboxylase - genetics
ADN
Amino Acid Sequence
Amino acids
Analytical, structural and metabolic biochemistry
Animals
Biological and medical sciences
Biosynthesis
Cloning, Molecular
CODE GENETIQUE
CODIGO GENETICO
COMPLEMENTARY DNA
DNA
DNA, Complementary - genetics
DNA, Plant - genetics
ENREGISTREMENT
Enzymes
Enzymes and enzyme inhibitors
Fundamental and applied biological sciences. Psychology
GENBANK/X81414
GENE
GENES
GENETIC CODE
Humans
LIASAS
LYASE
LYASES
MOLECULAR SEQUENCE DATA
NUCLEOTIDE SEQUENCE
Plant Gene Register
Polyamines
REGISTRATION
REGISTRO
SECUENCIA NUCLEOTIDICA
Sequence Homology, Amino Acid
SEQUENCE NUCLEOTIDIQUE
Spinach
SPINACIA OLERACEA
Spinacia oleracea - enzymology
Spinacia oleracea - genetics
Yeasts
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Description
Summary:S-Adenosylmethionine decarboxylase is an important enzyme in polyamine biosynthesis. It catalyzes the decarboxylation of S-adenosylmethionine, which serves as an aminopropyl donor for the conversion of putrescine to spermidine. A common feature of S-adenosylmethionine decarboxylases is that it is synthesized as a precursor molecule and is posttranslationally dissected to form two subunits ( alpha , beta ), which then together constitute the functional enzyme. As a result of this modification, a covalently linked prosthetic pyruvate group is generated from the N-terminal Ser residue at the cleavage site. One of the most important prerequisites to unraveling the function of spermidine is the availability of genes or cDNAs that encode enzymes of this biosynthesis pathway. Here we present the sequence of a full-length cDNA from spinach. Alignments of the protein sequence with those from yeast, rat, and human S-adenosylmethionine decarboxylases uncover five highly conserved segments of 9 to 16 amino acids in all of the enzymes strongly suggesting that the spinach cDNA encodes a S-adenosylmethionine decarboxylase.
ISSN:0032-0889
1532-2548
DOI:10.1104/pp.107.4.1461