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Merck

L3888

Sigma-Aldrich

D -莱氏乳杆菌乳酸脱氢酶

lyophilized powder, 150-500 units/mg protein

别名:

(R)-乳酸:NAD+ 氧化还原酶, D-LDH

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About This Item

CAS号:
EC號碼:
MDL號碼:
分類程式碼代碼:
12352204
NACRES:
NA.54

生物源

bacterial (Lactobacillus leichmannii)

品質等級

形狀

lyophilized powder

比活性

150-500 units/mg protein

成份

Protein, ~50% biuret

異物活動

Malic dehydrogenase <0.5% of base activity

儲存溫度

−20°C

一般說明

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. There are two types of D-LDHs: NAD-dependent D-LDHs and FAD-dependent D-LDHs.

應用

在食品工业,主要催化作用是将NADH和H+转化成NAD+ ,心肌黄酶将无荧光的刃天青转化成强荧光物质试卤灵,以测量食品中D-乳酸的含量。
D-Lactic Dehydrogenase from Lactobacillus leichmannii has been used:
  • in lactate dehydrogenase activity for testing the chaperone activity of proteins
  • to test the kinase activities of purified thiamine monophosphate(ThiM)
  • in NADH-coupled steady-state ATPase assay
  • to determine cellular lactate

生化/生理作用

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. Additionally, reduced D-LDH activity has been found in case of mutations in LDHD found in patients with D-lactic acidosis.
D-乳酸脱氢酶催化丙酮酸转化成 D-乳酸,同时将NADH氧化成NAD+。D-乳酸脱氢酶还可以催化逆反应,将D-乳酸转化成丙酮酸,同时将NAD+还原成NADH。

單位定義

D-乳酸脱氢酶催化丙酮酸转化成 D-乳酸,同时将NADH氧化成NAD+。 D-乳酸脱氢酶还可以催化逆反应,将 D-乳酸转化成丙酮酸,同时将NAD+ 还原成NADH。
在pH 7.0、25℃条件下,一单位酶每分钟可将1.0 μmM丙酮酸还原成D-乳酸。

外觀

含有磷酸缓冲盐的冻干粉

儲存類別代碼

11 - Combustible Solids

水污染物質分類(WGK)

WGK 3

閃點(°F)

Not applicable

閃點(°C)

Not applicable

個人防護裝備

Eyeshields, Gloves, type N95 (US)


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Zhaojuan Zheng et al.
Applied and environmental microbiology, 78(9), 3480-3483 (2012-02-22)
NAD-dependent l- and d-lactate dehydrogenases coexist in Lactobacillus genomes and may convert pyruvic acid into l-lactic acid and d-lactic acid, respectively. Our findings suggest that the relative catalytic efficiencies of ldhL- and ldhD-encoded products are crucial for the optical purity
Arnaud Mourier et al.
Biochimica et biophysica acta, 1777(10), 1283-1288 (2008-07-22)
Aerobically grown yeast cells express mitochondrial lactate dehydrogenases that localize to the mitochondrial inner membrane. The D-lactate dehydrogenase is a zinc-flavoprotein with high acceptor specificity for cytochrome c, that catalyzes the oxidation of D-lactate into pyruvate. In this paper, we
Andreas Neuner et al.
Biotechnology journal, 6(3), 318-329 (2011-03-04)
The Corynebacterium glutamicum ATCC 13032 lysC(fbr) strain was engineered to grow fast on racemic mixtures of lactate and to secrete lysine during growth on lactate as well as on mixtures of lactate and glucose. The wild-type C. glutamicum only grows
Takenori Shibahara et al.
Acta crystallographica. Section F, Structural biology and crystallization communications, 67(Pt 11), 1425-1427 (2011-11-22)
A dye-linked D-lactate dehydrogenase from the aerobic hyperthermophilic archaeon Aeropyrum pernix was crystallized using the hanging-drop vapour-diffusion method with polyethylene glycol 8000 as the precipitant. The crystals belonged to the monoclinic space group P2(1), with unit-cell parameters a = 63.4
Akos T Kovács et al.
Applied and environmental microbiology, 76(12), 4085-4088 (2010-04-20)
Bacillus coagulans has good potential as an industrial production organism for platform chemicals from renewable resources but has limited genetic tools available. Here, we present a targeted gene disruption system using the Cre-lox system, development of a LacZ reporter assay

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