| Properties of D(+)-lysopine dehydrogenase from crown gall tumour tissue. | |
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MedLine Citation:
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PMID: 21695 Owner: NLM Status: MEDLINE |
Abstract/OtherAbstract:
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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. |
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Authors:
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L A Otten; D Vreugdenhil; R A Schilperoort |
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Publication Detail:
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Type: Journal Article |
Journal Detail:
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Title: Biochimica et biophysica acta Volume: 485 ISSN: 0006-3002 ISO Abbreviation: Biochim. Biophys. Acta Publication Date: 1977 Dec |
Date Detail:
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Created Date: 1978-01-27 Completed Date: 1978-01-27 Revised Date: 2000-12-18 |
Medline Journal Info:
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Nlm Unique ID: 0217513 Medline TA: Biochim Biophys Acta Country: NETHERLANDS |
Other Details:
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Languages: eng Pagination: 268-77 Citation Subset: IM |
Export Citation:
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APA/MLA Format Download EndNote Download BibTex |
| MeSH Terms | |
Descriptor/Qualifier:
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Amino Acids
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analysis D-Amino-Acid Oxidase / isolation & purification, metabolism* Kinetics Lysine / analogs & derivatives Plant Tumors* Substrate Specificity |
| Chemical | |
Reg. No./Substance:
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0/Amino Acids; 56-87-1/Lysine; EC 1.4.3.3/D-Amino-Acid Oxidase |
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine
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