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
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Cofactor
Cofactor on EC 1.1.1.90 - aryl-alcohol dehydrogenase
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NAD+
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enzyme transfers hydride to the pro-R side of the prochiral C4 to the pyridine ring of NAD+
NAD+
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preferred cofactor compared to NADP+, all of the residues involved in cofactor binding are conserved. Residues Thr178 and Val203 interact with the nicotinamide ring, polypeptide backbone nitrogen atoms of residues Gly201 and Gly202 interact with an oxygen of the phosphate proximal to the nicotinamide group, and His47 binds the diphosphate of the NAD+ coenzyme. An Asp residue determines the specificity for NAD+
NADP+
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preferred cofactor is NAD+, all of the residues involved in cofactor binding are conserved. An Asp residue determines the specificity for NAD+
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contains no prosthetic group such as FAD or FMN
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