Document Detail


INTERACTION OF ASPARTATE AMINOTRANSFERASE WITH AMINO ACIDS.
MedLine Citation:
PMID:  14342499     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
1. The capacity of various amino acids to convert the pyridoxal form of aspartate aminotransferase into the pyridoxamine form has been investigated. 2. Glutamate has the highest converting capacity; aspartate, alpha-aminopimelate, alpha-aminoadipate and other amino acids follow. 3. The converting capacity of the various amino acids assayed is connected with their structural features. 4. A possible role of amino acids as secondary substrates of aspartate aminotransferase is suggested.
Authors:
P SCOTTO; V SCARDI
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Publication Detail:
Type:  Journal Article    
Journal Detail:
Title:  The Biochemical journal     Volume:  95     ISSN:  0264-6021     ISO Abbreviation:  Biochem. J.     Publication Date:  1965 Jun 
Date Detail:
Created Date:  1965-12-01     Completed Date:  1996-12-01     Revised Date:  2009-11-18    
Medline Journal Info:
Nlm Unique ID:  2984726R     Medline TA:  Biochem J     Country:  ENGLAND    
Other Details:
Languages:  eng     Pagination:  657-60     Citation Subset:  OM    
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MeSH Terms
Descriptor/Qualifier:
Adipic Acids
Aldehydes*
Amines*
Amino Acids*
Aspartate Aminotransferases*
Aspartic Acid*
Chemical Phenomena
Chemistry*
Glutamates*
Pimelic Acids*
Research*
Chemical
Reg. No./Substance:
0/Adipic Acids; 0/Aldehydes; 0/Amines; 0/Amino Acids; 0/Glutamates; 0/Pimelic Acids; 124-04-9/adipic acid; 56-84-8/Aspartic Acid; EC 2.6.1.1/Aspartate Aminotransferases
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