rdf:type |
|
lifeskim:mentions |
|
pubmed:issue |
1
|
pubmed:dateCreated |
1996-4-8
|
pubmed:abstractText |
The L-malate NAD(P)+ oxidoreductase (decarboxylating) E.C.1.1.1.39 was purified from human skeletal muscle; the specific activity estimated in the presence of NAPD+ as coenzyme was approximately 15 mumol/min/mg. The apparent Vmax values for NAD+ (approximately 8 mumol/min/mg) and NADP+ (approximately 16 mumol/min/mg) show that the enzyme (in this tissue) is more active in the presence of NAPD+. This observation was confirmed by the estimation of enzymatic activity in competition experiments where both NAD+ and NADP+ were used together as coenzymes. The absence of pyruvate carboxylation and of oxalacetate decarboxylation activities demonstrates that the enzyme studied is E.C.1.1.1.39. In addition, the apparent Km values for NAD+ and NADP+ were calculated (15 and 0.05 mM, respectively). This paper provides the first demonstration of a NADP+ preferring activity of the enzyme in human skeletal muscle.
|
pubmed:language |
eng
|
pubmed:journal |
|
pubmed:citationSubset |
IM
|
pubmed:chemical |
|
pubmed:status |
MEDLINE
|
pubmed:month |
Oct
|
pubmed:issn |
1077-3150
|
pubmed:author |
|
pubmed:issnType |
Print
|
pubmed:volume |
56
|
pubmed:owner |
NLM
|
pubmed:authorsComplete |
Y
|
pubmed:pagination |
14-8
|
pubmed:dateRevised |
2006-11-15
|
pubmed:meshHeading |
pubmed-meshheading:8593532-Carboxy-Lyases,
pubmed-meshheading:8593532-Chromatography, Affinity,
pubmed-meshheading:8593532-Chromatography, Ion Exchange,
pubmed-meshheading:8593532-Electrophoresis, Polyacrylamide Gel,
pubmed-meshheading:8593532-Humans,
pubmed-meshheading:8593532-Hydrogen-Ion Concentration,
pubmed-meshheading:8593532-Kinetics,
pubmed-meshheading:8593532-Malate Dehydrogenase,
pubmed-meshheading:8593532-Muscle, Skeletal,
pubmed-meshheading:8593532-NAD,
pubmed-meshheading:8593532-NADP,
pubmed-meshheading:8593532-Pyruvate Carboxylase
|
pubmed:year |
1995
|
pubmed:articleTitle |
NAD+/NADP+-dependent malic enzyme: evidence of a NADP+ preferring activity in human skeletal muscle.
|
pubmed:affiliation |
Research Laboratory of Service of Neuromuscular Diseases, San Camillo Hospital, Rome, Italy.
|
pubmed:publicationType |
Journal Article
|