It is a glycolytic enzyme responsible for converting pyruvate to lactate.
Enzymes are proteins that act as catalysts to speed up reactions.
LDH stands for lactate dehydrogenase, an enzyme found in the body that plays a role in the conversion of lactate to pyruvate during energy production. Elevated levels of LDH in the blood can indicate tissue damage or certain medical conditions.
The equation for the production of lactic acid after glycolysis is pyruvate + NADH + H+ -> lactate + NAD+. This reaction is catalyzed by the enzyme lactate dehydrogenase.
A LDH blood test measures the level of lactate dehydrogenase, an enzyme found in the body's tissues and organs. Elevated LDH levels may indicate tissue damage or diseases such as liver disease, heart attack, or certain types of cancer.
Alcohol dehydrogenase converts ethanol into acetaldehyde.
During intense exercise, when the body is low on oxygen, glucose is broken down into pyruvate through a process called glycolysis. Pyruvate is then converted into lactic acid by the enzyme lactate dehydrogenase in the muscles. This process helps regenerate NAD+ so that glycolysis can continue to produce energy in the absence of oxygen.
Correct answer: I, II, III and IV
lactate dehydrogenase
Lactate dehydrogenase is better known as lactic acid dehydrogenase. It is also abbreviated as LDH. If there is anything else it is called you can search for it on a medical website.
LDH stands for lactate dehydrogenase, an enzyme found in the body that plays a role in the conversion of lactate to pyruvate during energy production. Elevated levels of LDH in the blood can indicate tissue damage or certain medical conditions.
100 to 250 U/L
The equation for the production of lactic acid after glycolysis is pyruvate + NADH + H+ -> lactate + NAD+. This reaction is catalyzed by the enzyme lactate dehydrogenase.
Marc Beaudoin has written: 'Glucose, lactate and lactate dehydrogenase levels in the human kidney carcinoma cell line A498 (ATCC HTB-44)'
K. E. K. Rowson has written: 'Lactic dehydrogenase virus' -- subject(s): Lactate dehydrogenase virus, Unclassified Vertebrate viruses
Roman Sakowicz has written: 'Probing specificity determinants of the L-lactate dehydrogenase of Bacillus stearothermophilus'
Sandra Ostojic has written: 'A study of the Michaelis constant for the H4 and M4 isoenzymes of lactate dehydrogenase'
The vmax of lactate dehydrogenase (LDH) is the maximum velocity at which the enzyme can catalyze the conversion of lactate to pyruvate in a given concentration of substrate. This value represents the rate of the enzyme-catalyzed reaction at saturated substrate concentrations.
Lactate dehydrogenase (LDH or LD) is an enzyme (EC1.1.1.27) present in a wide variety of organisms, including plants and animals.Lactate dehydrogenases exist in four distinct enzyme classes. Two of them are cytochrome c-dependent enzymes, each acting on either D-lactate (EC 1.1.2.4) or L-lactate (EC 1.1.2.3). The other two are NAD(P)-dependent enzymes, each acting on either D-lactate (EC 1.1.1.28) or L-lactate (EC 1.1.1.27).