Document Detail


Essential arginine residues occur in or near the catalytic site of L-amino acid oxidase.
MedLine Citation:
PMID:  7095086     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
Butanedione in borate buffer irreversibly inactivates L-amino acid oxidase. L-Phenylalanine and L-methionine, which are good substrates for the enzyme, protect against inactivation but glycine, which is a very poor substrate, and D-phenylalanine which is neither substrate nor inhibitor, do not provide significant protection. These results are consistent with the modification by butanedione of one or more arginine residues located in or near the catalytic site of L-amino acid oxidase.
Authors:
M F Christman; J M Cardenas
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Publication Detail:
Type:  Journal Article; Research Support, U.S. Gov't, Non-P.H.S.; Research Support, U.S. Gov't, P.H.S.    
Journal Detail:
Title:  Experientia     Volume:  38     ISSN:  0014-4754     ISO Abbreviation:  Experientia     Publication Date:  1982 May 
Date Detail:
Created Date:  1982-09-24     Completed Date:  1982-09-24     Revised Date:  2007-11-14    
Medline Journal Info:
Nlm Unique ID:  0376547     Medline TA:  Experientia     Country:  SWITZERLAND    
Other Details:
Languages:  eng     Pagination:  537-8     Citation Subset:  IM    
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MeSH Terms
Descriptor/Qualifier:
Amino Acid Oxidoreductases / antagonists & inhibitors,  metabolism*
Arginine*
Binding Sites
Borates
Epoxy Compounds / pharmacology
Kinetics
L-Amino Acid Oxidase
Methionine / pharmacology
Phenylalanine / pharmacology
Stereoisomerism
Grant Support
ID/Acronym/Agency:
AM-25247/AM/NIADDK NIH HHS
Chemical
Reg. No./Substance:
0/Borates; 0/Epoxy Compounds; 1464-53-5/erythritol anhydride; 63-68-3/Methionine; 63-91-2/Phenylalanine; 74-79-3/Arginine; EC 1.4.-/Amino Acid Oxidoreductases; EC 1.4.3.2/L-Amino Acid Oxidase

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


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