1.1.1.90: aryl-alcohol dehydrogenase
This is an abbreviated version!
For detailed information about aryl-alcohol dehydrogenase, go to the full flat file.
Word Map on EC 1.1.1.90
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1.1.1.90
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benzaldehyde
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chrysosporium
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phanerochaete
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calcoaceticus
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xylene
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white-rot
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2,3-oxygenase
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aryl-aldehyde
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ligninolytic
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upper-pathway
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veratraldehyde
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veratryl
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n.c.i.b
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phenylglyoxylate
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biotechnology
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synthesis
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degradation
- 1.1.1.90
- benzaldehyde
-
chrysosporium
-
phanerochaete
- calcoaceticus
- xylene
-
white-rot
-
2,3-oxygenase
-
aryl-aldehyde
-
ligninolytic
-
upper-pathway
- veratraldehyde
-
veratryl
-
n.c.i.b
- phenylglyoxylate
- biotechnology
- synthesis
- degradation
Reaction
Synonyms
AADH, AC-BADH, ADH, ADP1, alcohol dehydrogenase, arylalcohol dehydrogenase, BADH, benzyl alcohol dehydrogenase, CADH, CADH II, coniferyl alcohol dehydrogenase, dehydrogenase, aryl alcohol, More, p-hydroxybenzyl alcohol dehydrogenase, TOL-BADH
ECTree
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Metals Ions
Metals Ions on EC 1.1.1.90 - aryl-alcohol dehydrogenase
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CaCl2
CdCl2
KBr
KCl
KNO3
Mg2+
MgCl2
NaCl
NH4Cl
Zn
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zinc-dependent alcohol dehydrogenase. All of the residues involved in zinc binding are conserved
Zn2+
additional information
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no effects on the enzyme activity by KCl, NaCl, and NiCl2, and by 10 mM urea and Tween-80
Zn2+
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dependent on, a catalytic zinc atom bound at the active site to the ligands Cys46, Asp49, His67, and Cys174 and a structural zinc atom bound to cysteine residues 97, 100, 103, and 111. All of the residues involved in zinc binding are conserved