1.2.1.65: salicylaldehyde dehydrogenase
This is an abbreviated version!
For detailed information about salicylaldehyde dehydrogenase, go to the full flat file.
Word Map on EC 1.2.1.65
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1.2.1.65
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salicylate
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naphthalene
-
dioxygenase
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catechol
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1,2-dihydroxynaphthalene
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naphthalene-degrading
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phenanthrene
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cis,cis-muconic
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trans-o-hydroxybenzylidenepyruvate
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gentisate
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catechol-1,2-dioxygenase
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pyrene
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1-hydroxy-2-naphthoic
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o-phthalate
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1-naphthol
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2-hydroxymuconic
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1,2-dioxygenase
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carbaryl
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coal
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dihydrodiol
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environmental protection
- 1.2.1.65
- salicylate
- naphthalene
- dioxygenase
- catechol
- 1,2-dihydroxynaphthalene
-
naphthalene-degrading
- phenanthrene
-
cis,cis-muconic
- trans-o-hydroxybenzylidenepyruvate
- gentisate
-
catechol-1,2-dioxygenase
- pyrene
-
1-hydroxy-2-naphthoic
- o-phthalate
- 1-naphthol
-
2-hydroxymuconic
-
1,2-dioxygenase
- carbaryl
-
coal
-
dihydrodiol
- environmental protection
Reaction
Synonyms
NAD+-dependent salicylaldehyde dehydrogenase, NahF, NahV, SAL dehydrogenase, SALD, SALDan, sALDH, salicylaldehyde dehydrogenase
ECTree
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Cofactor
Cofactor on EC 1.2.1.65 - salicylaldehyde dehydrogenase
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NAD+
amino acid residues Trp148, Phe226, Gly228, and Phe381 may bind NAD+, predicted binding mode based on modelling and molecular dynamic simulation. The adenine dinucleotide part of NAD+ is stabilized by Gly208, Glu209, Val212, Phe226, Gly228, Val232, Ile236, Glu379, and Phe381. The dinucleotide also forms a hydrogen bond with Lys172, Glu175, and Asn213. The nicotinamide of NAD+ interacts with Trp148 and Asn149 via hydrogen bond formation. Pro147, Leu251, and Gly252 contribute the binding by hydrophobic interactions. A conformational change occurred in the NAD+ binding site, which may facilitate NADH release