Document Detail

Properties of D(+)-lysopine dehydrogenase from crown gall tumour tissue.
MedLine Citation:
PMID:  21695     Owner:  NLM     Status:  MEDLINE    
D(+)-Lysopine dehydrogenase of an octopine-type Crown Gall tumour has been partially purified and a number of kinetic parameters have been determined. D(+)-Lysopine dehydrogenase catalyzes the reductive condensation of pyruvate and one of at least six different L-amino acids, as well as the reverse reactions, with preferential use of NADP(H) as a cofactor. The optimal pH for both reductive and oxidative reactions has been determined. At pH 6.8, L-lysine has of all the amino acids the lowest Km value, while at the same pH the highest V was found with L-arginine and L-histidine. The isoelectric point of D(+)-lysopine dehydrogenase is about 4.5.
L A Otten; D Vreugdenhil; R A Schilperoort
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Publication Detail:
Type:  Journal Article    
Journal Detail:
Title:  Biochimica et biophysica acta     Volume:  485     ISSN:  0006-3002     ISO Abbreviation:  Biochim. Biophys. Acta     Publication Date:  1977 Dec 
Date Detail:
Created Date:  1978-01-27     Completed Date:  1978-01-27     Revised Date:  2000-12-18    
Medline Journal Info:
Nlm Unique ID:  0217513     Medline TA:  Biochim Biophys Acta     Country:  NETHERLANDS    
Other Details:
Languages:  eng     Pagination:  268-77     Citation Subset:  IM    
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MeSH Terms
Amino Acids / analysis
D-Amino-Acid Oxidase / isolation & purification,  metabolism*
Lysine / analogs & derivatives
Plant Tumors*
Substrate Specificity
Reg. No./Substance:
0/Amino Acids; 56-87-1/Lysine; EC Oxidase

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

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