Document Detail


On the oxidation of cystathionamine and selenocystathionamine by plant amineoxidase.
MedLine Citation:
PMID:  8032325     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
Cystathionamine and selenocystathionamine, diamines analogous to 1,6-diaminohexane but having the third methylene group of the carbon chain substituted by a S or a Se atom, are asymmetrical thio- (seleno-) ethers. They can give rise by oxidative monodeamination to two different aminoaldehydes. It has been shown that lentil seedlings amineoxidase catalyzes the oxidative deamination of either the one or the other aminogroup of cystathionamine or of selenocystathionamine, giving rise to both possible aminoaldehydes.
Authors:
C Cini; C Blarzino; R Coccia; C Foppoli; C de Marco
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Publication Detail:
Type:  Comparative Study; Journal Article; Research Support, Non-U.S. Gov't    
Journal Detail:
Title:  Biochemistry and molecular biology international     Volume:  32     ISSN:  1039-9712     ISO Abbreviation:  Biochem. Mol. Biol. Int.     Publication Date:  1994 Mar 
Date Detail:
Created Date:  1994-08-16     Completed Date:  1994-08-16     Revised Date:  2006-11-15    
Medline Journal Info:
Nlm Unique ID:  9306673     Medline TA:  Biochem Mol Biol Int     Country:  AUSTRALIA    
Other Details:
Languages:  eng     Pagination:  575-84     Citation Subset:  IM    
Affiliation:
Dipartimento di Scienze Biochimiche A. Rossi Fanelli, Università La Sapienza, Roma, Italy.
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MeSH Terms
Descriptor/Qualifier:
Amine Oxidase (Copper-Containing)*
Cystathionine / analogs & derivatives*,  metabolism
Diamines / metabolism*
Kinetics
NAD / metabolism
Organoselenium Compounds / metabolism*
Oxidation-Reduction
Oxidoreductases Acting on CH-NH Group Donors / metabolism*
Oxygen Consumption
Plants / enzymology*
Substrate Specificity
Chemical
Reg. No./Substance:
0/Diamines; 0/Organoselenium Compounds; 53-84-9/NAD; 56-88-2/Cystathionine; 56973-49-0/cystathionamine; 58114-52-6/selenocystathionamine; EC 1.4.3.6/Amine Oxidase (Copper-Containing); EC 1.5.-/Oxidoreductases Acting on CH-NH Group Donors

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine


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