EzCatDB: D00001
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DB codeD00001
CATH domainDomain 13.90.180.10 : Quinone Oxidoreductase; Chain A, domain 1Catalytic domain
Domain 23.40.50.720 : Rossmann foldCatalytic domain
E.C.1.1.1.1
CSA1qlh
MACiEM0256

CATH domainRelated DB codes (homologues)
3.40.50.720 : Rossmann foldS00543,S00551,S00552,S00553,S00602,S00604,S00605,S00608,S00610,S00625,S00319,S00328,S00329,S00330,S00331,S00332,D00456,D00457,D00458,S00324,S00320,S00325,S00326,S00327,D00459,S00335,S00336,S00334,T00219,S00339,D00513,D00002,D00003,D00005,D00007,D00008,D00010,D00012,D00017,D00018,D00023,D00027,D00028,D00031,D00032,D00033,D00034,D00035,D00037,D00048,D00071,D00476,D00481,D00482,D00490,D00492,D00494,D00545,D00601,D00603,D00604,D00605,D00615,D00845,D00857,D00858,M00161,M00171,M00210,T00002,T00010,T00011,T00015,T00227,T00247,T00408,T00414,D00827,D00262,D00274,D00275,M00035,T00109
3.90.180.10 : Quinone Oxidoreductase; Chain A, domain 1D00002,D00018,D00048,D00481,D00482,D00490,D00492,D00615

Enzyme Name
UniProtKBKEGG

P00326P00327P00328
Protein nameAlcohol dehydrogenase 1CAlcohol dehydrogenase E chainAlcohol dehydrogenase S chainalcohol dehydrogenase
aldehyde reductase
ADH
alcohol dehydrogenase (NAD)
aliphatic alcohol dehydrogenase
ethanol dehydrogenase
NAD-dependent alcohol dehydrogenase
NAD-specific aromatic alcohol dehydrogenase
NADH-alcohol dehydrogenase
NADH-aldehyde dehydrogenase
primary alcohol dehydrogenase
yeast alcohol dehydrogenase
SynonymsEC 1.1.1.1
Alcohol dehydrogenase subunit gamma
EC 1.1.1.1
EC 1.1.1.1
RefSeqNP_000660.1 (Protein)
NM_000669.3 (DNA/RNA sequence)
NP_001075997.1 (Protein)
NM_001082528.1 (DNA/RNA sequence)
NP_001075414.1 (Protein)
NM_001081945.1 (DNA/RNA sequence)
PfamPF08240 (ADH_N)
PF00107 (ADH_zinc_N)
[Graphical view]
PF08240 (ADH_N)
PF00107 (ADH_zinc_N)
[Graphical view]
PF08240 (ADH_N)
PF00107 (ADH_zinc_N)
[Graphical view]

KEGG pathways
MAP codePathways
MAP00010Glycolysis / Gluconeogenesis
MAP00071Fatty acid metabolism
MAP00120Bile acid biosynthesis
MAP00260Glycine, serine and threonine metabolism
MAP00350Tyrosine metabolism
MAP006241- and 2-Methylnaphthalene degradation
MAP006413-Chloroacrylic acid degradation
MAP00830Retinol metabolism
MAP00980Metabolism of xenobiotics by cytochrome P450
MAP00982Drug metabolism - cytochrome P450

UniProtKB:Accession NumberP00326P00327P00328
Entry nameADH1G_HUMANADH1E_HORSEADH1S_HORSE
ActivityAn alcohol + NAD(+) = an aldehyde or ketone + NADH.An alcohol + NAD(+) = an aldehyde or ketone + NADH.An alcohol + NAD(+) = an aldehyde or ketone + NADH.
SubunitDimer of identical or non-identical chains of three types, alpha, beta and gamma.Dimer of identical or non-identical chains of two types (E and S) coded by 2 separate genes at different loci.Dimer of identical or non-identical chains of two types (E and S) coded by 2 separate genes at different loci.
Subcellular locationCytoplasm.Cytoplasm.Cytoplasm.
CofactorBinds 2 zinc ions per subunit.Binds 2 zinc ions per subunit.Binds 2 zinc ions per subunit (By similarity).

Compound table: links to PDB-related databases & PoSSuM

CofactorsSubstratesProducts
KEGG-idC00038C00003C00226C00069C00004C00071C00709C00080
CompoundZincNAD+Primary alcoholAlcoholNADHAldehydeKetoneH+
Typeheavy metalamide group,amine group,nucleotidecarbohydratecarbohydrateamide group,amine group,nucleotidecarbohydratecarbohydrateothers
ChEBI29105
15846


16908


15378
PubChem32051
5893


439153


1038
                
1ht0A01Bound:2x_ZNUnboundUnboundUnboundUnboundUnboundUnbound 
1ht0B01Bound:2x_ZNUnboundUnboundUnboundUnboundUnboundUnbound 
1a71A01Bound:2x_ZNUnboundAnalogue:ETFUnboundUnboundUnboundUnbound 
1a71B01Bound:2x_ZNUnboundAnalogue:ETFUnboundUnboundUnboundUnbound 
1a72A01Bound:2x_ZNUnboundUnboundUnboundUnboundUnboundUnbound 
1adbA01Bound:2x_ZNUnboundBound:EOHUnboundUnboundUnboundUnbound 
1adbB01Bound:2x_ZNUnboundBound:EOHUnboundUnboundUnboundUnbound 
1adcA01Bound:2x_ZNUnboundBound:EOHUnboundUnboundUnboundUnbound 
1adcB01Bound:2x_ZNUnboundBound:EOHUnboundUnboundUnboundUnbound 
1adfA01Bound:2x_ZNUnboundUnboundUnboundUnboundUnboundUnbound 
1adgA01Bound:2x_ZNUnboundUnboundUnboundUnboundUnboundUnbound 
1axeA01Bound:2x_ZNUnboundAnalogue:ETFUnboundUnboundUnboundUnbound 
1axeB01Bound:2x_ZNUnboundAnalogue:ETFUnboundUnboundUnboundUnbound 
1axgA01Bound:2x_ZNUnboundAnalogue:ETFUnboundUnboundUnboundUnbound 
1axgB01Bound:2x_ZNUnboundAnalogue:ETFUnboundUnboundUnboundUnbound 
1axgC01Bound:2x_ZNUnboundAnalogue:ETFUnboundUnboundUnboundUnbound 
1axgD01Bound:2x_ZNUnboundAnalogue:ETFUnboundUnboundUnboundUnbound 
1btoA01Bound:2x_ZNUnboundUnboundUnboundUnboundUnboundAnalogue:SSB 
1btoB01Bound:2x_ZNUnboundUnboundUnboundUnboundUnboundAnalogue:SSB 
1btoC01Bound:2x_ZNUnboundUnboundUnboundUnboundUnboundAnalogue:SSB 
1btoD01Bound:2x_ZNUnboundUnboundUnboundUnboundUnboundAnalogue:SSB 
1hetA01Bound:2x_ZNUnboundUnboundBound:MRDUnboundUnboundUnbound 
1hetB01Bound:2x_ZNUnboundUnboundBound:MRDUnboundUnboundUnbound 
1heuA01Analogue:2x_CDUnboundUnboundBound:MRDUnboundUnboundUnbound 
1heuB01Analogue:2x_CDUnboundUnboundBound:MRDUnboundUnboundUnbound 
1hldA01Bound:2x_ZNUnboundAnalogue:PFB,BRBUnboundUnboundUnboundUnbound 
1hldB01Bound:2x_ZNUnboundAnalogue:PFB,BRBUnboundUnboundUnboundUnbound 
1ju9A01Bound:2x_ZNUnboundUnboundUnboundUnboundUnboundUnbound 
1ju9B01Bound:2x_ZNUnboundUnboundUnboundUnboundUnboundUnbound 
1ldeA01Bound:2x_ZNUnboundUnboundUnboundUnboundAnalogue:FPIUnbound 
1ldeB01Bound:2x_ZNUnboundUnboundUnboundUnboundAnalogue:FPIUnbound 
1ldeC01Bound:2x_ZNUnboundUnboundUnboundUnboundAnalogue:FPIUnbound 
1ldeD01Bound:2x_ZNUnboundUnboundUnboundUnboundAnalogue:FPIUnbound 
1ldyA01Bound:2x_ZNUnboundUnboundUnboundUnboundAnalogue:CXFUnbound 
1ldyB01Bound:2x_ZNUnboundUnboundUnboundUnboundAnalogue:CXFUnbound 
1ldyC01Bound:2x_ZNUnboundUnboundUnboundUnboundAnalogue:CXFUnbound 
1ldyD01Bound:2x_ZNUnboundUnboundUnboundUnboundAnalogue:CXFUnbound 
1mg0A01Bound:2x_ZNUnboundAnalogue:DFBUnboundUnboundUnboundUnbound 
1mg0B01Bound:2x_ZNUnboundAnalogue:DFBUnboundUnboundUnboundUnbound 
1mg0C01Bound:2x_ZNUnboundAnalogue:DFBUnboundUnboundUnboundUnbound 
1mg0D01Bound:2x_ZNUnboundAnalogue:DFBUnboundUnboundUnboundUnbound 
1mgoA01Bound:2x_ZNUnboundUnboundUnboundUnboundUnboundUnbound 
1mgoB01Bound:2x_ZNUnboundUnboundBound:MPDUnboundUnboundUnbound 
1n8kA01Bound:2x_ZNUnboundUnboundUnboundUnboundUnboundUnbound 
1n8kB01Bound:2x_ZNUnboundUnboundUnboundUnboundUnboundUnbound 
1n92A01Bound:2x_ZNUnboundUnboundUnboundUnboundUnboundUnbound 
1n92B01Bound:2x_ZNUnboundUnboundUnboundUnboundUnboundUnbound 
1p1rA01Bound:2x_ZNUnboundUnboundUnboundUnboundAnalogue:NMHUnbound 
1p1rB01Bound:2x_ZNUnboundUnboundUnboundUnboundAnalogue:NMHUnbound 
1p1rC01Bound:2x_ZNUnboundUnboundUnboundUnboundAnalogue:NMHUnbound 
1p1rD01Bound:2x_ZNUnboundUnboundUnboundUnboundAnalogue:NMHUnbound 
1qlhA01Bound:2x_ZNUnboundUnboundUnboundUnboundUnboundUnbound 
1qljA01Bound:2x_ZNUnboundUnboundUnboundUnboundUnboundUnbound 
1qv6A01Bound:2x_ZNUnboundAnalogue:24BUnboundUnboundUnboundUnbound 
1qv6B01Bound:2x_ZNUnboundAnalogue:24BUnboundUnboundUnboundUnbound 
1qv7A01Bound:2x_ZNUnboundAnalogue:DFBUnboundUnboundUnboundUnbound 
1qv7B01Bound:2x_ZNUnboundAnalogue:DFBUnboundUnboundUnboundUnbound 
2ohxA01Bound:2x_ZNUnboundUnboundUnboundUnboundUnboundAnalogue:DMS 
2ohxB01Bound:2x_ZNUnboundUnboundUnboundUnboundUnboundAnalogue:DMS 
2oxiA01Bound:_ZN,Analogue;_CUUnboundUnboundUnboundUnboundUnboundAnalogue:DMS 
2oxiB01Bound:_ZN,Analogue;_CUUnboundUnboundUnboundUnboundUnboundAnalogue:DMS 
3btoA01Bound:2x_ZNUnboundUnboundUnboundUnboundUnboundAnalogue:SSB 
3btoB01Bound:2x_ZNUnboundUnboundUnboundUnboundUnboundAnalogue:SSB 
3btoC01Bound:2x_ZNUnboundUnboundUnboundUnboundUnboundAnalogue:SSB 
3btoD01Bound:2x_ZNUnboundUnboundUnboundUnboundUnboundAnalogue:SSB 
5adhA01Bound:2x_ZNUnboundUnboundBound:MPDUnboundUnboundUnbound 
6adhA01Bound:2x_ZNUnboundUnboundUnboundUnboundUnboundAnalogue:DMS 
6adhB01Bound:2x_ZNUnboundUnboundUnboundUnboundUnboundAnalogue:DMS 
7adhA01Bound:2x_ZNUnboundUnboundUnboundUnboundUnboundUnbound 
8adhA01Bound:2x_ZNUnboundUnboundUnboundUnboundUnboundUnbound 
1ee2A01Bound:2x_ZNUnboundUnboundUnboundUnboundUnboundAnalogue:CHD 
1ee2B01Bound:2x_ZNUnboundUnboundUnboundUnboundUnboundAnalogue:CHD 
1ht0A02UnboundBound:NADUnboundUnboundUnboundUnboundUnbound 
1ht0B02UnboundBound:NADUnboundUnboundUnboundUnboundUnbound 
1a71A02UnboundBound:NADUnboundUnboundUnboundUnboundUnbound 
1a71B02UnboundBound:NADUnboundUnboundUnboundUnboundUnbound 
1a72A02UnboundAnalogue:PADUnboundUnboundUnboundUnboundUnbound 
1adbA02UnboundAnalogue:CNDUnboundUnboundUnboundUnboundUnbound 
1adbB02UnboundAnalogue:CNDUnboundUnboundUnboundUnboundUnbound 
1adcA02UnboundAnalogue:PADUnboundUnboundUnboundUnboundUnbound 
1adcB02UnboundAnalogue:PADUnboundUnboundUnboundUnboundUnbound 
1adfA02UnboundAnalogue:TADUnboundUnboundUnboundUnboundUnbound 
1adgA02UnboundAnalogue:SADUnboundUnboundUnboundUnboundUnbound 
1axeA02UnboundBound:NADUnboundUnboundUnboundUnboundUnbound 
1axeB02UnboundBound:NADUnboundUnboundUnboundUnboundUnbound 
1axgA02UnboundBound:NADUnboundUnboundUnboundUnboundUnbound 
1axgB02UnboundBound:NADUnboundUnboundUnboundUnboundUnbound 
1axgC02UnboundBound:NADUnboundUnboundUnboundUnboundUnbound 
1axgD02UnboundBound:NADUnboundUnboundUnboundUnboundUnbound 
1btoA02UnboundUnboundUnboundUnboundBound:NADUnboundUnbound 
1btoB02UnboundUnboundUnboundUnboundBound:NADUnboundUnbound 
1btoC02UnboundUnboundUnboundUnboundBound:NADUnboundUnbound 
1btoD02UnboundUnboundUnboundUnboundBound:NADUnboundUnbound 
1hetA02UnboundBound:NADUnboundUnboundBound:NADUnboundUnbound 
1hetB02UnboundBound:NADUnboundUnboundBound:NADUnboundUnbound 
1heuA02UnboundBound:NADUnboundUnboundBound:NADUnboundUnbound 
1heuB02UnboundBound:NADUnboundUnboundBound:NADUnboundUnbound 
1hldA02UnboundBound:NADAnalogue:PFB,BRBUnboundUnboundUnboundUnbound 
1hldB02UnboundBound:NADAnalogue:PFB,BRBUnboundUnboundUnboundUnbound 
1ju9A02UnboundAnalogue:NADUnboundUnboundUnboundUnboundUnbound 
1ju9B02UnboundAnalogue:NADUnboundUnboundUnboundUnboundUnbound 
1ldeA02UnboundUnboundUnboundUnboundBound:NADUnboundUnbound 
1ldeB02UnboundUnboundUnboundUnboundBound:NADUnboundUnbound 
1ldeC02UnboundUnboundUnboundUnboundBound:NADUnboundUnbound 
1ldeD02UnboundUnboundUnboundUnboundBound:NADUnboundUnbound 
1ldyA02UnboundUnboundUnboundUnboundBound:NADUnboundUnbound 
1ldyB02UnboundUnboundUnboundUnboundBound:NADUnboundUnbound 
1ldyC02UnboundUnboundUnboundUnboundBound:NADUnboundUnbound 
1ldyD02UnboundUnboundUnboundUnboundBound:NADUnboundUnbound 
1mg0A02UnboundBound:NADUnboundUnboundUnboundUnboundUnbound 
1mg0B02UnboundBound:NADUnboundUnboundUnboundUnboundUnbound 
1mg0C02UnboundBound:NADUnboundUnboundUnboundUnboundUnbound 
1mg0D02UnboundBound:NADUnboundUnboundUnboundUnboundUnbound 
1mgoA02UnboundBound:NADUnboundUnboundUnboundUnboundUnbound 
1mgoB02UnboundBound:NADUnboundUnboundUnboundUnboundUnbound 
1n8kA02UnboundAnalogue:NAJ-PZOUnboundUnboundUnboundUnboundUnbound 
1n8kB02UnboundAnalogue:NAJ-PZOUnboundUnboundUnboundUnboundUnbound 
1n92A02UnboundAnalogue:NAJ-PYZUnboundUnboundUnboundUnboundUnbound 
1n92B02UnboundAnalogue:NAJ-PYZUnboundUnboundUnboundUnboundUnbound 
1p1rA02UnboundUnboundUnboundUnboundBound:NAJUnboundUnbound 
1p1rB02UnboundUnboundUnboundUnboundBound:NAJUnboundUnbound 
1p1rC02UnboundUnboundUnboundUnboundBound:NAJUnboundUnbound 
1p1rD02UnboundUnboundUnboundUnboundBound:NAJUnboundUnbound 
1qlhA02UnboundBound:NADUnboundUnboundUnboundUnboundUnbound 
1qljA02UnboundUnboundUnboundUnboundUnboundUnboundUnbound 
1qv6A02UnboundBound:NADUnboundUnboundUnboundUnboundUnbound 
1qv6B02UnboundBound:NADUnboundUnboundUnboundUnboundUnbound 
1qv7A02UnboundBound:NADUnboundUnboundUnboundUnboundUnbound 
1qv7B02UnboundBound:NADUnboundUnboundUnboundUnboundUnbound 
2ohxA02UnboundUnboundUnboundUnboundBound:NADUnboundUnbound 
2ohxB02UnboundUnboundUnboundUnboundBound:NADUnboundUnbound 
2oxiA02UnboundUnboundUnboundUnboundBound:NADUnboundUnbound 
2oxiB02UnboundUnboundUnboundUnboundBound:NADUnboundUnbound 
3btoA02UnboundUnboundUnboundUnboundBound:NADUnboundUnbound 
3btoB02UnboundUnboundUnboundUnboundBound:NADUnboundUnbound 
3btoC02UnboundUnboundUnboundUnboundBound:NADUnboundUnbound 
3btoD02UnboundUnboundUnboundUnboundBound:NADUnboundUnbound 
5adhA02UnboundAnalogue:APRUnboundUnboundUnboundUnboundUnbound 
6adhA02UnboundBound:NADUnboundUnboundUnboundUnboundUnbound 
6adhB02UnboundBound:NADUnboundUnboundUnboundUnboundUnbound 
7adhA02UnboundUnboundUnboundUnboundUnboundUnboundUnbound 
8adhA02UnboundUnboundUnboundUnboundUnboundUnboundUnbound 
1ee2A02UnboundBound:NADUnboundUnboundUnboundUnboundUnbound 
1ee2B02UnboundBound:NADUnboundUnboundUnboundUnboundUnbound 

Active-site residues
resource
Swiss-prot;P00327, P00326, P00328,P26325
pdbCatalytic residuesCofactor-binding residuescomment
           
1ht0A01SER 48;HIS 51
CYS 46;HIS 67;CYS 174(Catalytic zinc binding)
mutant I349V
1ht0B01SER 48;HIS 51
CYS 46;HIS 67;CYS 174(Catalytic zinc binding)
mutant I349V
1a71A01SER 48;HIS 51
CYS 46;HIS 67;CYS 174(Catalytic zinc binding)
mutant F93W
1a71B01SER 48;HIS 51
CYS 46;HIS 67;CYS 174(Catalytic zinc binding)
mutant F93W
1a72A01SER 48;HIS 51
CYS 46;HIS 67;CYS 174(Catalytic zinc binding)
mutant F93W
1adbA01SER 48;HIS 51
CYS 46;HIS 67;CYS 174(Catalytic zinc binding)
 
1adbB01SER 48;HIS 51
CYS 46;HIS 67;CYS 174(Catalytic zinc binding)
 
1adcA01SER 48;HIS 51
CYS 46;HIS 67;CYS 174(Catalytic zinc binding)
 
1adcB01SER 48;HIS 51
CYS 46;HIS 67;CYS 174(Catalytic zinc binding)
 
1adfA01SER 48;HIS 51
CYS 46;HIS 67;CYS 174(Catalytic zinc binding)
 
1adgA01SER 48;HIS 51
CYS 46;HIS 67;CYS 174(Catalytic zinc binding)
 
1axeA01SER 48;HIS 51
CYS 46;HIS 67;CYS 174(Catalytic zinc binding)
mutant F93W
1axeB01SER 48;HIS 51
CYS 46;HIS 67;CYS 174(Catalytic zinc binding)
mutant F93W
1axgA01SER 48;HIS 51
CYS 46;HIS 67;CYS 174(Catalytic zinc binding)
 
1axgB01SER 48;HIS 51
CYS 46;HIS 67;CYS 174(Catalytic zinc binding)
 
1axgC01SER 48;HIS 51
CYS 46;HIS 67;CYS 174(Catalytic zinc binding)
 
1axgD01SER 48;HIS 51
CYS 46;HIS 67;CYS 174(Catalytic zinc binding)
 
1btoA01SER 48;HIS 51
CYS 46;HIS 67;CYS 174(Catalytic zinc binding)
 
1btoB01SER 48;HIS 51
CYS 46;HIS 67;CYS 174(Catalytic zinc binding)
 
1btoC01SER 48;HIS 51
CYS 46;HIS 67;CYS 174(Catalytic zinc binding)
 
1btoD01SER 48;HIS 51
CYS 46;HIS 67;CYS 174(Catalytic zinc binding)
 
1hetA01SER 48;HIS 51
CYS 46;HIS 67;CYS 174(Catalytic zinc binding)
 
1hetB01SER 48;HIS 51
CYS 46;HIS 67;CYS 174(Catalytic zinc binding)
 
1heuA01SER 48;HIS 51
CYS 46;HIS 67;CYS 174(Catalytic zinc binding)
 
1heuB01SER 48;HIS 51
CYS 46;HIS 67;CYS 174(Catalytic zinc binding)
 
1hldA01SER 48;HIS 51
CYS 46;HIS 67;CYS 174(Catalytic zinc binding)
 
1hldB01SER 48;HIS 51
CYS 46;HIS 67;CYS 174(Catalytic zinc binding)
 
1ju9A01SER 48;HIS 51
CYS 46;HIS 67;CYS 174(Catalytic zinc binding)
 
1ju9B01SER 48;HIS 51
CYS 46;HIS 67;CYS 174(Catalytic zinc binding)
 
1ldeA01SER 48;HIS 51
CYS 46;HIS 67;CYS 174(Catalytic zinc binding)
 
1ldeB01SER 48;HIS 51
CYS 46;HIS 67;CYS 174(Catalytic zinc binding)
 
1ldeC01SER 48;HIS 51
CYS 46;HIS 67;CYS 174(Catalytic zinc binding)
 
1ldeD01SER 48;HIS 51
CYS 46;HIS 67;CYS 174(Catalytic zinc binding)
 
1ldyA01SER 48;HIS 51
CYS 46;HIS 67;CYS 174(Catalytic zinc binding)
 
1ldyB01SER 48;HIS 51
CYS 46;HIS 67;CYS 174(Catalytic zinc binding)
 
1ldyC01SER 48;HIS 51
CYS 46;HIS 67;CYS 174(Catalytic zinc binding)
 
1ldyD01SER 48;HIS 51
CYS 46;HIS 67;CYS 174(Catalytic zinc binding)
 
1mg0A01SER 48;HIS 51
CYS 46;HIS 67;CYS 174(Catalytic zinc binding)
mutant F93A
1mg0B01SER 48;HIS 51
CYS 46;HIS 67;CYS 174(Catalytic zinc binding)
mutant F93A
1mg0C01SER 48;HIS 51
CYS 46;HIS 67;CYS 174(Catalytic zinc binding)
mutant F93A
1mg0D01SER 48;HIS 51
CYS 46;HIS 67;CYS 174(Catalytic zinc binding)
mutant F93A
1mgoA01SER 48;HIS 51
CYS 46;HIS 67;CYS 174(Catalytic zinc binding)
mutant F93A
1mgoB01SER 48;HIS 51
CYS 46;HIS 67;CYS 174(Catalytic zinc binding)
mutant F93A
1n8kA01SER 48;HIS 51
CYS 46;HIS 67;CYS 174(Catalytic zinc binding)
 
1n8kB01SER 48;HIS 51
CYS 46;HIS 67;CYS 174(Catalytic zinc binding)
 
1n92A01SER 48;HIS 51
CYS 46;HIS 67;CYS 174(Catalytic zinc binding)
 
1n92B01SER 48;HIS 51
CYS 46;HIS 67;CYS 174(Catalytic zinc binding)
 
1p1rA01SER 48;HIS 51
CYS 46;HIS 67;CYS 174(Catalytic zinc binding)
 
1p1rB01SER 48;HIS 51
CYS 46;HIS 67;CYS 174(Catalytic zinc binding)
 
1p1rC01SER 48;HIS 51
CYS 46;HIS 67;CYS 174(Catalytic zinc binding)
 
1p1rD01SER 48;HIS 51
CYS 46;HIS 67;CYS 174(Catalytic zinc binding)
 
1qlhA01SER 48;HIS 51
CYS 46;HIS 67;CYS 174(Catalytic zinc binding)
 
1qljA01SER 48;HIS 51
CYS 46;HIS 67;CYS 174(Catalytic zinc binding)
 
1qv6A01SER 48;      
CYS 46;HIS 67;CYS 174(Catalytic zinc binding)
mutant H51Q
1qv6B01SER 48;      
CYS 46;HIS 67;CYS 174(Catalytic zinc binding)
mutant H51Q
1qv7A01SER 48;      
CYS 46;HIS 67;CYS 174(Catalytic zinc binding)
mutant H51Q
1qv7B01SER 48;      
CYS 46;HIS 67;CYS 174(Catalytic zinc binding)
mutant H51Q
2ohxA01SER 48;HIS 51
CYS 46;HIS 67;CYS 174(Catalytic zinc binding)
 
2ohxB01SER 48;HIS 51
CYS 46;HIS 67;CYS 174(Catalytic zinc binding)
 
2oxiA01SER 48;HIS 51
CYS 46;HIS 67;CYS 174(Catalytic zinc binding)
 
2oxiB01SER 48;HIS 51
CYS 46;HIS 67;CYS 174(Catalytic zinc binding)
 
3btoA01SER 48;HIS 51
CYS 46;HIS 67;CYS 174(Catalytic zinc binding)
 
3btoB01SER 48;HIS 51
CYS 46;HIS 67;CYS 174(Catalytic zinc binding)
 
3btoC01SER 48;HIS 51
CYS 46;HIS 67;CYS 174(Catalytic zinc binding)
 
3btoD01SER 48;HIS 51
CYS 46;HIS 67;CYS 174(Catalytic zinc binding)
 
5adhA01SER 48;HIS 51
CYS 46;HIS 67;CYS 174(Catalytic zinc binding)
 
6adhA01SER 48;HIS 51
CYS 46;HIS 67;CYS 174(Catalytic zinc binding)
 
6adhB01SER 48;HIS 51
CYS 46;HIS 67;CYS 174(Catalytic zinc binding)
 
7adhA01SER 48;HIS 51
CYS 46;HIS 67;CYS 174(Catalytic zinc binding)
 
8adhA01SER 48;HIS 51
CYS 46;HIS 67;CYS 174(Catalytic zinc binding)
 
1ee2A01SER 48;HIS 51
CYS 46;HIS 67;CYS 173(Catalytic zinc binding)
 
1ee2B01SER 48;HIS 51
CYS 46;HIS 67;CYS 173(Catalytic zinc binding)
 
1ht0A02 
 
mutant R271Q
1ht0B02 
 
mutant R271Q
1a71A02 
 
mutant V203A
1a71B02 
 
mutant V203A
1a72A02 
 
mutant V203A
1adbA02 
 
 
1adbB02 
 
 
1adcA02 
 
 
1adcB02 
 
 
1adfA02 
 
 
1adgA02 
 
 
1axeA02 
 
 
1axeB02 
 
 
1axgA02 
 
mutant V203A
1axgB02 
 
mutant V203A
1axgC02 
 
mutant V203A
1axgD02 
 
mutant V203A
1btoA02 
 
 
1btoB02 
 
 
1btoC02 
 
 
1btoD02 
 
 
1hetA02 
 
 
1hetB02 
 
 
1heuA02 
 
 
1heuB02 
 
 
1hldA02 
 
 
1hldB02 
 
 
1ju9A02 
 
mutant V292S
1ju9B02 
 
mutant V292S
1ldeA02 
 
 
1ldeB02 
 
 
1ldeC02 
 
 
1ldeD02 
 
 
1ldyA02 
 
 
1ldyB02 
 
 
1ldyC02 
 
 
1ldyD02 
 
 
1mg0A02 
 
 
1mg0B02 
 
 
1mg0C02 
 
 
1mg0D02 
 
 
1mgoA02 
 
 
1mgoB02 
 
 
1n8kA02 
 
mutant V292T
1n8kB02 
 
mutant V292T
1n92A02 
 
 
1n92B02 
 
 
1p1rA02 
 
 
1p1rB02 
 
 
1p1rC02 
 
 
1p1rD02 
 
 
1qlhA02 
 
mutant G293A, P295T
1qljA02 
 
mutant G293A, P295T
1qv6A02 
 
mutant K228R
1qv6B02 
 
mutant K228R
1qv7A02 
 
mutant K228R
1qv7B02 
 
mutant K228R
2ohxA02 
 
 
2ohxB02 
 
 
2oxiA02 
 
 
2oxiB02 
 
 
3btoA02 
 
 
3btoB02 
 
 
3btoC02 
 
 
3btoD02 
 
 
5adhA02 
 
 
6adhA02 
 
 
6adhB02 
 
 
7adhA02 
 
 
8adhA02 
 
 
1ee2A02 
 
 
1ee2B02 
 
 

References for Catalytic Mechanism
ReferencesSectionsNo. of steps in catalysis
[4]Scheme 1, p.14356-14357
[10]Fig.4, p.1065-1067
[13]Fig.2, p.619-621, p.624-625
[31]Fig.10, p.5235-5237
[32]p.273
[41]Fig.2, p.9786-9789, p.9790-9791
[42]p.135-136
[53]Scheme 1, p.13957-13959
[57]Chart 1, Chart 2, p.11955-11956, p.11957-11959
[58]Fig.5, p.9320
[60]Scheme 2, p.480
[67]Scheme 1, p.3023-3025
[70]Fig.7, p.3930

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PubMed ID1544927
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PubMed ID8493927
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PubMed ID8218182
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[25]
PubMed ID8490046
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[26]
PubMed ID7684231
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[27]
PubMed ID8354263
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CommentsX-ray crystallography
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[31]
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PubMed ID8172897
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Year1994
Volume33
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Related PDB1hld
[32]
PubMed ID8032158
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Year1994
Volume71
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PubMed ID7766625
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PubMed ID7479907
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[47]
CommentsX-ray crystallography
PubMed ID9003191
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Related PDB1bto,3bto
[48]
CommentsX-ray crystallography
PubMed ID9132002
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Related PDB1lde,1ldy
[49]
CommentsX-ray crystallography
PubMed ID9371755
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Related PDB1axe,1axg
[50]
PubMed ID9521768
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Volume37
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[51]
CommentsX-ray crystallography
PubMed ID9649310
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Volume37
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Related PDB1a71,1a72
[52]
PubMed ID9485460
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Year1998
Volume37
Pages3068-77
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[53]
CommentsX-ray crystallography
PubMed ID10529241
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Year1999
Volume38
Pages13951-9
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Related PDB1qlh,1qlj
[54]
CommentsX-ray crystallography
PubMed ID11041853
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Year2000
Volume39
Pages12885-97
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Related PDB1ee2
[55]
CommentsTheoretical model
PubMed ID10733557
JournalHepatology
Year2000
Volume31
Pages990-6
AuthorsMarschall HU, Oppermann UC, Svensson S, Nordling E, Persson B, Hoog JO, Jornvall H
TitleHuman liver class I alcohol dehydrogenase gammagamma isozyme: the sole cytosolic 3beta-hydroxysteroid dehydrogenase of iso bile acids.
Related PDB1dda
[56]
CommentsX-ray crystallography
PubMed ID11601993
JournalBiochemistry
Year2001
Volume40
Pages12686-94
AuthorsRubach JK, Ramaswamy S, Plapp BV
TitleContributions of valine-292 in the nicotinamide binding site of liver alcohol dehydrogenase and dynamics to catalysis.
Related PDB1ju9
[57]
PubMed ID11724603
JournalJ Am Chem Soc
Year2001
Volume123
Pages11952-9
AuthorsLuo J, Bruice TC
TitleDynamic structures of horse liver alcohol dehydrogenase (HLADH): results of molecular dynamics simulations of HLADH-NAD(+)-PhCH(2)OH, HLADH-NAD(+)-PhCH(2)O(-), and HLADH-NADH-PhCHO.
[58]
CommentsX-ray crystallography
PubMed ID11134046
JournalJ Biol Chem
Year2001
Volume276
Pages9316-21
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TitleOn the enzymatic activation of NADH.
Related PDB1het,1heu
[59]
CommentsX-ray crystallography
PubMed ID11274460
JournalProtein Sci
Year2001
Volume10
Pages697-706
AuthorsNiederhut MS, Gibbons BJ, Perez-Miller S, Hurley TD
TitleThree-dimensional structures of the three human class I alcohol dehydrogenases.
Related PDB1hso,1hsz,1ht0
[60]
PubMed ID12491384
JournalAngew Chem Int Ed Engl
Year2002
Volume41
Pages478-81
AuthorsLo HC, Fish RH
TitleBiomimetic NAD(+) models for tandem cofactor regeneration, horse liver alcohol dehydrogenase recognition of 1,4-NADH derivatives, and chiral synthesis.
[61]
CommentsX-ray crystallography
PubMed ID12501206
JournalBiochemistry
Year2002
Volume41
Pages15770-9
AuthorsRubach JK, Plapp BV
TitleMobility of fluorobenzyl alcohols bound to liver alcohol dehydrogenases as determined by NMR and X-ray crystallographic studies.
Related PDB1mg0,1mgo
[62]
PubMed ID11916410
JournalJ Am Chem Soc
Year2002
Volume124
Pages3270-6
AuthorsCaratzoulas S, Mincer JS, Schwartz SD
TitleIdentification of a protein-promoting vibration in the reaction catalyzed by horse liver alcohol dehydrogenase.
[63]
PubMed ID11942822
JournalJ Am Chem Soc
Year2002
Volume124
Pages3858-64
AuthorsKohen A, Jensen JH
TitleBoundary conditions for the Swain-Schaad relationship as a criterion for hydrogen tunneling.
[64]
PubMed ID12481026
JournalProc Natl Acad Sci U S A
Year2002
Volume99
Pages16597-600
AuthorsLuo J, Bruice TC
TitleTen-nanosecond molecular dynamics simulation of the motions of the horse liver alcohol dehydrogenase.PhCH2O- complex.
[65]
CommentsX-ray crystallography
PubMed ID12627956
JournalBiochemistry
Year2003
Volume42
Pages2907-15
AuthorsRubach JK, Plapp BV
TitleAmino acid residues in the nicotinamide binding site contribute to catalysis by horse liver alcohol dehydrogenase.
Related PDB1n8k,1n92
[66]
CommentsX-ray crystallography
PubMed ID12855684
JournalJ Biol Chem
Year2003
Volume278
Pages36699-706
AuthorsVenkataramaiah TH, Plapp BV
TitleFormamides mimic aldehydes and inhibit liver alcohol dehydrogenases and ethanol metabolism.
Related PDB1p1r
[67]
CommentsX-ray crystallography
PubMed ID15023053
JournalBiochemistry
Year2004
Volume43
Pages3014-26
AuthorsLeBrun LA, Park DH, Ramaswamy S, Plapp BV
TitleParticipation of histidine-51 in catalysis by horse liver alcohol dehydrogenase.
Related PDB1qv6,1qv7
[68]
PubMed ID15331786
JournalProc Natl Acad Sci U S A
Year2004
Volume101
Pages13152-6
AuthorsLuo J, Bruice TC
TitleAnticorrelated motions as a driving force in enzyme catalysis: the dehydrogenase reaction.
[69]
PubMed ID15449945
JournalBiochemistry
Year2004
Volume43
Pages12555-62
AuthorsGibbons BJ, Hurley TD
TitleStructure of three class I human alcohol dehydrogenases complexed with isoenzyme specific formamide inhibitors.
Related PDB1u3t
[70]
PubMed ID19011748
JournalCell Mol Life Sci
Year2008
Volume65
Pages3918-35
AuthorsLadenstein R, Winberg JO, Benach J
TitleMedium- and short-chain dehydrogenase/reductase gene and protein families : Structure-function relationships in short-chain alcohol dehydrogenases.

comments
This enzyme belongs to the class I of the zinc-containing alcohol dehydrogenase superfamily.
Although this enzyme binds two zinc ions, only one zinc is involved in catalysis.
According to the literature [4], [10] and [70], the hydride transfer reaction proceeds as follows:
(0) Catalytic zinc ion, which is bound to Cys46, His67 and Cys174 and the hydroxyl group of the substrate alcohol, may lower the pKa of the hydroxyl oxygen of the alcohol, facilitating its deprotonation.
(1) His51 may act as a general base to deprotonate the hydroxyl oxygen, through 2'-hydroxyl group of NAD+ ribose and Ser48 by a proton relay system, leading to an alkoxide transition-state.
(2) The pro-R hydrogen is transferred from the carbon atom of alcohol to the nicotinamide group in the NAD+. Thus, hydride transfer occurs.

createdupdated
2005-01-112010-09-08


Copyright: Nozomi Nagano, JST & CBRC-AIST
Funded by PRESTO/Japan Science and Technology Corporation (JST) (December 2001 - November 2004)
Funded by Grant-in-Aid for Publication of Scientific Research Results/Japan Society for the Promotion of Science (JSPS) (April 2005 - March 2006)
Funded by Grant-in-Aid for Scientific Research (B)/Japan Society for the Promotion of Science (JSPS) (April 2005 - March 2008)
Funded by BIRD/Japan Science and Technology Corporation (JST) (September 2005 - September 2008)
Funded by BIRD/Japan Science and Technology Corporation (JST) (October 2007 - September 2010)
Funded by Grant-in-Aid for Publication of Scientific Research Results/Japan Society for the Promotion of Science (JSPS) (April 2011 - March 2012)
Funded by Grant-in-Aid for Publication of Scientific Research Results/Japan Society for the Promotion of Science (JSPS) (April 2012 - March 2013)
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