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??? ????? ??? ???
?? ??:
9031-72-5
???:
??? ?????
???(??):
????????;????????(ALCOHOLDEHYDROGENASE(FROMEQUINELIVER))
???:
EC 1.1.1.1
???(??):
ADH;LKADH;HLADH;EC 1.1.1.1;EC: 1.1.1.1;IUB: 1.1.1.1;ADH, Alcohol:;KETOREDUCTASE CB;KETOREDUCTASE CP;KETOREDUCTASE RS1
CBNumber:
CB9358485
???:
n.a.
??? ??:
0
MOL ??:
Mol file
MSDS ??:
SDS

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RTECS ??
SZ5999500
?? ??
-20°C
???
H2O: ??? 1.0mg/mL, ????? ?? ???, ?? ?? ??? ???
??? ??
??
??
?? ???
??????(pH)
7
???? ??
Saccharomyces cerevisiae
???
?? ?????.
??
Hygroscopic
Specific Activity
≥300units/mg protein
EPA
Dehydrogenase, alcohol (9031-72-5)
??
  • ?? ? ?? ??
  • ?? ? ???? ?? (GHS)
WGK ?? 3
F ?????? 3-10-21
TSCA Yes
HS ?? 35079090
???? ?? KE-09577
????(GHS): GHS hazard pictograms
?? ?: Danger
??·?? ??:
?? ??·?? ?? ?? ?? ?? ?? ? ?? ?? P- ??
H317 ????? ?? ??? ??? ? ?? ?? ??? ?? ?? 1 ?? GHS hazard pictograms P261, P272, P280, P302+P352,P333+P313, P321, P363, P501
H334 ?? ? ????? ??, ?? ?? ?? ?? ?? ??? ? ?? ??? ??? ?? ?? 1 ?? GHS hazard pictograms P261, P285, P304+P341, P342+P311,P501
??????:
P261 ??·?·??·???·??·...·????? ??? ????.
P272 ??? ??? ??? ??? ???? ???.
P280 ????/???/???/?????? ?????.
P285 ??? ? ?? ?? ???? ??? ???? ?????
P302+P352 ??? ??? ??? ?? ????.
P304+P341 ???? ??,??? ??? ?? ??? ??? ??? ?? ??? ??? ???? ?? ??? ??? ??? ?
P321 (…) ??? ???.
P333+P313 ????? ?? ??? ???? ???? ??·??? ????.
P342+P311 ??? ??? ???? ????(??)? ??? ????.
P363 ?? ??? ??? ??? ?????.
P501 ...? ??? / ??? ?? ???.
NFPA 704
1
0 1

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Alcohol dehydrogenase catalyzes the reaction: RCH2OH +NAD+ ? RCHO + NADH + H+ It facilitates the interconversion between alcohols and aldehydes or ketones with the reduction of nicotinamide adenine dinucleotide (NAD+ to NADH). In biotransformation, alcohol dehydrogenases are often used for the synthesis of enantiomerically pure stereoisomers of chiral alcohols.

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This product has been enhanced for energy efficiency and waste prevention when used in fuel cell research.

Biochem/physiol Actions

Alcohol dehydrogenase catalyzes the oxidative conversion of alcohol into aldehyde. It has a homodimeric structure with a co-enzyme binding domain at the C-terminal and an N-terminal catalytic domain. The active site is located at the interdomain cleft. Binding of NAD+ in the active site causes conformational changes which create the binding site for the alcohol substrate.

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