1.2.1.9: glyceraldehyde-3-phosphate dehydrogenase (NADP+)

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

Word Map on EC 1.2.1.9

Reaction

D-glyceraldehyde 3-phosphate
+
NADP+
+
H2O
=
3-phospho-D-glycerate
+
NADPH
+ 2 H+

Synonyms

apo-GAPDH, apo-glyceraldehyde-3-phosphate dehydrogenase, dehydrogenase, glyceraldehyde phosphate (nicotinamide adenine dinucleotide phosphate), E268A-GAPN, GAP dehydrogenase, GAPDH, GAPDH (A4), GAPDHN, GAPN, glyceraldehyde 3-phosphate dehydrogenase, glyceraldehyde 3-phosphate dehydrogenase (NADP), glyceraldehyde 3-phosphate:NADP+ reductase, non-phosphorylating, glyceraldehyde phosphate dehydrogenase (NADP), glyceraldehyde-3-phosphate dehydrogenase, glyceraldehyde-3-phosphate dehydrogenase (NADP+), Glyceraldehyde-3-phosphate dehydrogenase [NADP+], glyceraldehyde-3-phosphate:NADP reductase, NADP+-dependent GAPDH, NADP+-dependent glyceraldehyde 3-phosphate dehydrogenase, NADP+-GAPDH, NADP-dependent glyceraldehyde-3-phosphate dehydrogenase, NADP-dependent nonphosphorylating glyceraldehyde-3-phosphate dehydrogenase, NADP-glyceraldehyde phosphate dehydrogenase, NADP-glyceraldehyde-3-phosphate dehydrogenase, NADPH-dependent GAPDH, NADPH-glyceraldehyde-3-phosphate dehydrogenase, non phosphorylating glyceraldehyde-3-phosphate dehydrogenase, non-phosphorylating GAP dehydrogenase, Non-phosphorylating glyceraldehyde 3-phosphate dehydrogenase, non-phosphorylating glyceraldehyde-3-phosphate dehydrogenase, non-phosphorylating glyceraldehyde-3-phosphate dehydrogenase GAPN, non-phosphorylating NADP+-dependent Ga3PDHase, non-phosphorylating NADP+-dependent glyceraldehyde-3-phosphate dehydrogenase, non-phosphorylating NADP-dependent glyceraldehyde-3-phosphate dehydrogenase, nonphosphorylating glyceraldehyde-3-phosphate dehydrogenase, nonphosphorylating NADP-dependent glyceraldehyde-3-phosphate dehydrogenase, NP-Ga3PDHase, NP-GAPDH, OsALDH11, SSO3194, St-GAPN, STK_24770, triose phosphate dehydrogenase, Triosephosphate dehydrogenase

ECTree

     1 Oxidoreductases
         1.2 Acting on the aldehyde or oxo group of donors
             1.2.1 With NAD+ or NADP+ as acceptor
                1.2.1.9 glyceraldehyde-3-phosphate dehydrogenase (NADP+)

Engineering

Engineering on EC 1.2.1.9 - glyceraldehyde-3-phosphate dehydrogenase (NADP+)

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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
R190A
-
the catalytic constant, kcat, of the mutant in the presence of NADH decreases 10fold while the Km for NADH decreases 12fold. The mutant shows no activity with NADPH
R82A
-
the mutation leads to a 10fold increase in the Km for NADPH but does not affect the kinetics of NADH
R82D
-
the mutation leads to a 10fold increase in the Km for NADPH but does not affect the kinetics of NADH
S195A
-
the mutation has no effect on the affinity of the enzyme for NADPH and its affinity for NADH and for BPGA in the presence of NADH is reduced
A(plusCTE)
-
chimeric mutant for testing the regulatory function of CTE
B(E326Q)
-
site specific mutant of the GAPDH B-subunit
B(minCTE)
-
deletion mutant for testing the regulatory function of CTE
B(R77A)
-
site specific mutant of the GAPDH B-subunit
B(S188A)
-
site specific mutant of the GAPDH B-subunit
C302A
-
compared to wild-type enzyme the amount of the thermolabile species is higher
E268A
E268Q
-
attacking water molecule in the hydrolysis process is poorly activated, can be overcome by the nulceophiles hydrazin and hydroxylamine
N169T
-
compared to wild-type enzyme the amount of the thermolabile species is significantly lower
R124L
-
turnover number is 21fold lower than turnover-number of wild-type enzym
R301L
-
turnover number is 1000fold lower than turnover-number of wild-type enzyme. Rate limiting step is acylation, compared to deacylation in wild-type enzyme
R459I
T195G
-
compared to wild-type enzyme the amount of the thermolabile species is similar
Y170F
-
turnover number is 1.7fold higher than turnover-number of wild-type enzyme
A198S/S199I
-
the catalytic efficiency with NADP+ decreases while that with NAD+ increases by 2.5fold. Substitutions reduces the NADP/NAD preference ratio by more than 50%; the mutant shows reduced catalytic efficiency with NADP+ and increased catalytic efficiency with NAD+ as compared to the wild type enzyme
E141D
-
kcat for D-glyceraldehyde 3-phosphate is 2.1fold lower than wild-type value
K137E
-
kcat for D-glyceraldehyde 3-phosphate is 1.1fold lower than wild-type value
L138T
-
kcat for D-glyceraldehyde 3-phosphate is 1.3fold lower than wild-type value
R136K
-
kcat for D-glyceraldehyde 3-phosphate is 2.8fold lower than wild-type value
S199I
-
the catalytic efficiency (kcat/Km) with NADP+ decreases by 0.5fold while that with NAD+ remains unchanged. Substitution reduces the NADP/NAD preference ratio by more than 50%; the mutant shows reduced catalytic efficiency with NADP+ and increased catalytic efficiency with NAD+ as compared to the wild type enzyme
Y139R
-
kcat for D-glyceraldehyde 3-phosphate is 302fold lower than wild-type value. The mutant enzyme no longer displays a sigmoidal K-type-like allostery but instead has apparent V-type allostery similar to that of the Sulfolobus solfataricus enzyme, suggesting that the residue located in the center of the homotetramer critically contributes to the allosteric behavior
A198S/S199I
-
the catalytic efficiency with NADP+ decreases while that with NAD+ increases by 2.5fold. Substitutions reduces the NADP/NAD preference ratio by more than 50%
-
E141D
-
kcat for D-glyceraldehyde 3-phosphate is 2.1fold lower than wild-type value
-
K137E
-
kcat for D-glyceraldehyde 3-phosphate is 1.1fold lower than wild-type value
-
L138T
-
kcat for D-glyceraldehyde 3-phosphate is 1.3fold lower than wild-type value
-
R136K
-
kcat for D-glyceraldehyde 3-phosphate is 2.8fold lower than wild-type value
-
S199I
-
the catalytic efficiency (kcat/Km) with NADP+ decreases by 0.5fold while that with NAD+ remains unchanged. Substitution reduces the NADP/NAD preference ratio by more than 50%
-
additional information