1.4.1.7: serine 2-dehydrogenase
This is an abbreviated version!
For detailed information about serine 2-dehydrogenase, go to the full flat file.
Word Map on EC 1.4.1.7
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1.4.1.7
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nadp+-dependent
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tumefaciens
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dehydrogenases
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semialdehyde
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1.4.1.14
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agrobacterium
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constantly
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nadh-glutamate
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d-serine
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nadp+
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synthases
- 1.4.1.7
-
nadp+-dependent
- tumefaciens
- dehydrogenases
- semialdehyde
-
1.4.1.14
-
agrobacterium
-
constantly
-
nadh-glutamate
- d-serine
- nadp+
- synthases
Reaction
Synonyms
L-serine:NAD oxidoreductase (deaminating), NAD+-dependent L-serine dehydrogenase, protein PA0743, serine dehydrogenase
ECTree
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Subunits
Subunits on EC 1.4.1.7 - serine 2-dehydrogenase
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additional information
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the enzyme has an N-terminal Rossmann fold domain connected by a long alpha-helix to the C-terminal all-alpha domain. Critical role of four amino acid residues in catalysis including the primary catalytic residue Lys171, PA0743 substrate-binding site structure, and molecular mechanisms of substrate selectivity, overview. The structure of the PA0743-NAD+ complex demonstrates that the opposite side of the enzyme active site accommodates the cofactor, which is also bound near Lys171, with dinucleotide cofactor binding GLGXMG motif-1, substrate binding DAPVSGG motif-2, catalysis GXXGXGXXXKXXN motif-3, and cofactor binding motif-4