L3888
D-Lactic Dehydrogenase from Lactobacillus leichmannii
lyophilized powder, 150-500 units/mg protein
Sinónimos:
(R)-Lactate:NAD+ oxidoreductase, D-LDH
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origen biológico
bacterial (Lactobacillus leichmannii)
Nivel de calidad
Formulario
lyophilized powder
actividad específica
150-500 units/mg protein
composición
Protein, ~50% biuret
actividad extraña
Malic dehydrogenase <0.5% of base activity
temp. de almacenamiento
−20°C
Categorías relacionadas
Descripción general
Research area: Cell Signaling
Lactate Dehydrogenase (LDH) is classified as an oxidoreductase and is found in various organisms, including both plants and animals. LDH is widely distributed across all tissues, with high concentrations in muscle, kidney, and liver. The genes encoding LDH are LDHA, LDHB, LDHC, and LDHD. The D-isomer is produced by LDHD.[1] There are two types of D-LDHs: NAD-dependent D-LDHs and FAD-dependent D-LDHs.[2]
Lactate Dehydrogenase (LDH) is classified as an oxidoreductase and is found in various organisms, including both plants and animals. LDH is widely distributed across all tissues, with high concentrations in muscle, kidney, and liver. The genes encoding LDH are LDHA, LDHB, LDHC, and LDHD. The D-isomer is produced by LDHD.[1] There are two types of D-LDHs: NAD-dependent D-LDHs and FAD-dependent D-LDHs.[2]
Aplicación
D-Lactic Dehydrogenase from Lactobacillus leichmannii has been used:
In the food industry, the primary catalysis is coupled to conversion of NADH and H+ to NAD+ with diaphorase coupled with converting the non-fluorescent resazurin to the highly fluorescent substance resorufin to measure the content of D-lactate in food products.
Acciones bioquímicas o fisiológicas
D-lactic dehydrogenase catalyzes the conversion of pyruvate into D-lactate, with oxidation of NADH to NAD+. D-lactic dehydrogenase can also catalyze the reverse reaction, conversion of D-lactate into pyruvate with reduction of NAD+ to NADH.
It acts as a crucial checkpoint in gluconeogenesis and DNA metabolism. Elevated levels of LDH in the blood have been observed in various conditions, including heart attacks, cancers, liver disease, muscle trauma, anemia, bone fractures, and infections such as encephalitis, human immunodeficiency virus(HIV), and meningitis. LDH also serves as a non-specific marker of tissue turnover, which is a normal metabolic process.[1] Additionally, reduced D-LDH activity has been found in case of mutations in LDHD found in patients with D-lactic acidosis.[2]
Definición de unidad
D-lactic dehydrogenase catalyzes the conversion of pyruvate into D-lactate, with oxidation of NADH to NAD+. D-lactic dehydrogenase can also catalyze the reverse reaction, conversion of D-lactate into pyruvate with reduction of NAD+ to NADH.
One unit will reduce 1.0 μmole of pyruvate to D-lactate per min at pH 7.0 at 25 °C.
Forma física
Lyophilized powder containing phosphate buffer salts
Código de clase de almacenamiento
11 - Combustible Solids
Clase de riesgo para el agua (WGK)
WGK 3
Punto de inflamabilidad (°F)
Not applicable
Punto de inflamabilidad (°C)
Not applicable
Equipo de protección personal
Eyeshields, Gloves, type N95 (US)
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