ChemicalBook--->CAS DataBase List--->9001-18-7

9001-18-7

9001-18-7 Structure

9001-18-7 Structure
IdentificationBack Directory
[Name]

DIAPHORASE
[CAS]

9001-18-7
[Synonyms]

QR1
DTD
NQO1
DHQU
DIA4
NMOR1
232-587-6
EC 1.6.99
DTD HUMAN
DIAPHORASE
EC: 1.6.99
EC 1.8.1.4
EC 1.6.99.2
E.C. 1.6.4.3
IUB: 1.6.99.1
DT DIAPHORASE
QUINONE REDUCTASE
DT DIAPHORASE HUMAN
EC 1.8.1.4 TYPE III
Lipoamide reductase
DIAPHORASE etrapure
LIPOYL DEHYDROGENASE
DIAPHORASE USP/EP/BP
Lipoate dehydrogenase
QUINONE REDUCTASE HUMAN
LIPOAMIDE DEHYDROGENASE
Dehydrogenase, lipoamide
NADH: DYE OXIDOREDUCTASE
Lipoamide oxidoreductase
Lipoic acid dehydrogenase
Dihydrolipoic dehydrogenase
Dihydrolipoyl dehydrogenase
Dihydrolipoate dehydrogenase
Dihydrothioctic dehydrogenase
alpha-Lipoamide dehydrogenase
Dihydrolipoamide dehydrogenase
Lipoamide dehydrogenase (NADH)
NADH: LIPOAMIDE OXIDOREDUCTASE
DiaphoraseExClostridiumKluyveri
LIPOAMIDE DEHYDROGENASE TYPE III
NAD(P)H: ACCEPTOR OXIDOREDUCTASE
DIHYDROLIPOAMIDE: NAD OXIDOREDUCTASE
DIAPHORASE FROM CLOSTRIDIUM KLUYVERI
Diaphorase from E. coli, Recombinant
Diaphorase 22 from Recombinant E.coli
DIHYDROLIPOAMIDE: NAD+ OXIDOREDUCTASE
Native Clostridium kluyveri Diaphorase
Diaphorase ex. Clostridium Sp., 30U/mg
NADH: LIPOAMIDE OXIDOREDUCTASE TYPE III
LIPOAMIDE DEHYDROGENASE FROM BOVINE INTE
LIPOAMIDE DEHYDROGENASE TYPE III FROM PO
lipoamide dehydrogenase from porcine heart
DIAPHORASE, FROM CLOSTRIDIUM KLUYVERI, TYPE III
Monoclonal Anti-NQO1 antibody produced in mouse
LIPOAMIDE DEHYDROGENASE TYPE V FROM TORU LA YEAST
lipoamide dehydrogenase from bovine intestinal mucosa
Diaphorase from Clostridium kluyveri, ≥25 units/mg dry weight
NAD(P)H dehydrogenase (quinone), NAD(P)H: (quinone-acceptor) oxidoreductase
[EINECS(EC#)]

232-587-6
[MDL Number]

MFCD00130947
Chemical PropertiesBack Directory
[storage temp. ]

-20°C
[form ]

lyophilized powder
[color ]

light brown-yellow
[biological source]

mouse
[Specific Activity]

3.0-20.0units/mg protein (biuret)
[EPA Substance Registry System]

Dehydrogenase, lipoamide (9001-18-7)
Safety DataBack Directory
[Hazard Codes ]

Xi
[Risk Statements ]

36/37/38
[Safety Statements ]

26-36
[WGK Germany ]

3
[F ]

3-10
[TSCA ]

Yes
[HS Code ]

3507909090
[Storage Class]

13 - Non Combustible Solids
Hazard InformationBack Directory
[Uses]

Diaphorase from Clostridium kluyveri has been used in lactate dehydrogenase assay in gill cells and impregnated on the strip for formate dehydrogenase assay.
[Uses]

Methylene blue (MB)-containing polyacrylamide nanoparticle platforms (NPs) were tested in solution with diaphorase from Clostridium kluyveri and the cofactor NADH. this test done done to check whether the encapsulation of MB in NPs could prevent the reduction of MB, and thus protect its photodynamic effectiveness. The enzyme from Sigma has been used along with aldehyde dehydrogenase to construct a biosensor for acetaldehyde by immobilization. It has also been used in the reoxidation of NADP to NADPH. This reaction simultaneously catalyzed the conversion of resazurin into the highly fluorescent resorufin, and also allowed the detection of minute amounts of NAADP. NAADP was initially converted to NADP and NADPH by other enzymes.
[Uses]

Diaphorase from Clostridium kluyveri, or Lipoyl dehydrogenase, has been used in a study to assess the protein-protein interactions in assembly of lipoic acid on the 2-oxoacid dehydrogenases of aerobic metabolism. Lipoyl dehydrogenase has also been used in a study to investigate the redox regulation of tyrosine nitration and 3-nitrotyrosine reduction by antioxidants.
[Biochem/physiol Actions]

Diaphorase catalyzes the oxidation of either β-NADH or β-NADPH in the presence of an electron acceptor such as methylene blue or 2,6-dichlorophenolindophenol. Diaphorases which are specific for either β-NADH or β-NADPH are known. The pig heart enzyme of Straub seems to have native diaphorase (β-NADH specific) as well as lipoic and lipoamide dehydrogenase activities. It is reported to be a single protein. However, Massey reports that diaphorase is probably a denatured lipoamide dehydrogenase. Pre-incubation of the pig heart preparation with Cu2+ reduces the lipoamide dehydrogenase activity and proportionately increases the β-NADH diaphorase activity. In our laboratory, we have demonstrated this copper effect to some degree on the pig heart enzyme, but no appreciable effect was observed on the Clostridium kluyveri or torula yeast preparations. The lipoamide dehydrogenase:diaphorase ratio is a measure of the denaturation.
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