1.2.1.13: glyceraldehyde-3-phosphate dehydrogenase (NADP+) (phosphorylating)

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

Word Map on EC 1.2.1.13

Reaction

D-glyceraldehyde 3-phosphate
+
phosphate
+
NADP+
=
3-phospho-D-glyceroyl phosphate
+
NADPH
+
H+

Synonyms

A2B2-GAPDH, A2B2-glyceraldehyde-3-phosphate dehydrogenase, A4 glyceraldehyde 3-phosphate dehydrogenase, A4-GAPDH, D-glyceraldehyde-3-phosphate dehydrogenase, dehydrogenase, glyceraldehyde phosphate (nicotinamide adenine dinucleotide phosphate phosphorylating), GapA, GapA-1, GapB, GAPC, GAPD, GAPDH, GAPDH (A4), glyceraldehyde 3-phosphate dehydrogenase (NADP), glyceraldehyde phosphate dehydrogenase (nicotinamide adenine dinucleotide phosphate phosphorylating), glyceraldehyde-3-dehydrogenase, glyceraldehyde-3-P dehydrogenase, glyceraldehyde-3-phosphate dehhydrogenase (NADP+) (phoshphorylating), glyceraldehyde-3-phosphate dehydrogenase, glyceraldehyde-3-phosphate dehydrogenase (NADP+), glyceraldehyde-P dehydrogenase, GraP-DH, NAD(P)-GAPDH, NADP(H)-glyceraldehyde-3-phosphate dehydrogenase, NADP+-dependent G-3-P dehydrogenase, NADP+-dependent gapB, NADP+-dependent glyceraldehyde-3-phosphate dehydrogenase, NADP+-GAPDH, NADP-dependent GAPDH, NADP-dependent glyceradehdye-3-phosphate dehydrogenase, NADP-dependent glyceraldehyde 3-phosphate dehydrogenase, NADP-dependent glyceraldehyde phosphate dehydrogenase, NADP-dependent glyceraldehydephosphate dehydrogenase, NADP-GAPDH, NADP-glyceraldehyde phosphate dehydrogenase, NADP-glyceraldehyde-3-phosphate dehydrogenase, NADP-GPD, NADP-triose phosphate dehydrogenase, NADPH-D-GA3P, NADPH-glyceraldehyde-3-phosphate dehydrogenase, NAPD-linked glyceraldehyde-3-P dehydrogenase, Ov-GAPDH, phosphorylating GAP dehydrogenase, phosphorylating glyceraldehyde-3-phosphate dehydrogenase, photosynthetic GAPDH, SSO0528, triosephosphate dehydrogenase (NADP+)

ECTree

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

Engineering

Engineering on EC 1.2.1.13 - glyceraldehyde-3-phosphate dehydrogenase (NADP+) (phosphorylating)

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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
K128A
-
Km-value for NADPH is nearly identical to wild-type value, turnover-number for NADPH is decreased about 2fold. Km-value for NADH is increased 2.1fold compared to wild-type enzyme, turnover-number for NADH is decreased 2.6fold
K128E
-
Km-value for NADPH is about 80% of the wild-type value, turnover-number for NADPH is decreased 2.7fold. Km-value for NADH is increased 2.3fold compared to wild-type enzyme, turnover-number for NADH is decreased 1.9fold
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
R197A
-
Km-value for NADPH is identical to wild-type value, turnover-number for NADPH is about 90% of the wild-type value. Km-value for NADH is about 80% of the wild-type value, turnover-number for NADH is nearly identical to wild-type value
R197E
-
Km-value for NADPH is increased 1.3fold compared to wild-type enzyme, turnover-number for NADPH is decreased 2fold. Km-value for NADH is about 90% of the wild-type value, turnover-number for NADH is increased 1.3fold
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
C151S
K225A
-
K225 is critical for binding of GAPDH to Siah1, an ubiquitin-E3-ligase, eliciting the translocation of GAPDH to the nucleus
Y123W
-
increase of temperature of irreversible inactivation by 1.3°C
Y323S
-
decrease of temperature of irreversible inactivation by 4.5°C
C151S
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
C18S
-
mutant of GapB subunit still shows stron redox regulation
C274S
-
mutant of GapB subunit still shows stron redox regulation
C285S
-
mutant of GapB subunit still shows stron redox regulation
C349S
-
mutant of GapB subunit is less redox-sensitive than GapB. Active tetramer, unable to aggregate to higher oligomers in presence of NAD+
C349S/C358S
-
mutant of GapB subunit is less redox-sensitive than GapB. Active tetramer, unable to aggregate to higher oligomers in presence of NAD+
c358S
-
mutant of GapB subunit is less redox-sensitive than GapB. Active tetramer, unable to aggregate to higher oligomers in presence of NAD+
D351N
the mutation only marginally affects the redox sensitivity
E356Q
the mutation only marginally affects the redox sensitivity
E356Q/E357Q
complete redox insensitivity is achieved in the double mutant
E357Q
the mutation only marginally affects the redox sensitivity
S188A
affinity for NADPH is significantly decreased, decrease in the ratio of turnover number to Km-value in the NADPH-dependent reaction, significant expansion of the A4-tetramer
T33A
affinity for NADPH is significantly decreased, turnover-number for NADPH is lowered
T33A/S188A
affinity for NADPH is significantly decreased, turnover-number for NADPH is lowered
additional information