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1.1.1.387: L-serine 3-dehydrogenase (NAD+)

This is an abbreviated version!
For detailed information about L-serine 3-dehydrogenase (NAD+), go to the full flat file.

Reaction

2-aminomalonate semialdehyde
=
2-aminoacetaldehyde
+
CO2

Synonyms

L-SerDH, L-serine 3-dehydrogenase, L-serine dehydrogenase, NAD+-dependent L-serine dehydrogenase, PA0743

ECTree

     1 Oxidoreductases
         1.1 Acting on the CH-OH group of donors
             1.1.1 With NAD+ or NADP+ as acceptor
                1.1.1.387 L-serine 3-dehydrogenase (NAD+)

Substrates Products

Substrates Products on EC 1.1.1.387 - L-serine 3-dehydrogenase (NAD+)

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SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
2-aminomalonate semialdehyde
2-aminoacetaldehyde + CO2
show the reaction diagram
-
spontaneous
-
-
?
3-hydroxypropionate + NAD+
? + NADH + H+
show the reaction diagram
-
-
-
-
?
D-glycerate + NAD+
?
show the reaction diagram
-
-
-
?
D-serine + NAD+
2-aminoacetaldehyde + CO2 + NADH + H+
show the reaction diagram
-
overall reaction, 5% of the relative activity observed with L-serine
-
-
?
DL-3-hydroxyisobutyrate + NAD+
? + NADH + H+
show the reaction diagram
-
-
-
-
?
DL-glycerate + NAD+
? + NADH + H+
show the reaction diagram
-
-
-
-
?
DL-threonine + NAD+
?
show the reaction diagram
-
-
-
?
L-serine + NAD(P)+
2-aminomalonate semialdehyde + NAD(P)H + H+
show the reaction diagram
-
-
-
-
?
L-serine + NAD+
2-aminoacetaldehyde + CO2 + NADH + H+
show the reaction diagram
-
overall reaction, NAD+ is the preferred cofactor
-
-
?
L-serine + NAD+
?
show the reaction diagram
L-serine + NADP+
2-aminoacetaldehyde + CO2 + NADPH + H+
show the reaction diagram
-
overall reaction, low activity with NADP+
-
-
?
methyl 2,2-dimethyl-3-hydroxypropionate + NAD+
?
show the reaction diagram
-
-
-
?
additional information
?
-
-
modeling of the D-serine and 3-hydroxypropionate molecules into the enzyme's active site. No steric hindrance is observed between D-serine and the side chains of the active site residues. D-serine is placed at the position through interactions similar to the L-serine binding model. The C3 hydrogen of D-serine is located at the same position as that of L-serine. This may explain the high reactivity toward D-serine exhibited by Pyrobaculum calidifontis L-SerDH
-
-
-