1.1.1.79: glyoxylate reductase (NADP+)
This is an abbreviated version!
For detailed information about glyoxylate reductase (NADP+), go to the full flat file.
Reaction
Synonyms
aac4036, At3g25530, AtGLYR1, AtGLYR2, AtGR1, AtGR2, D-2-hydroxy-acid dehydrogenase, GhrA, glycerate dehydrogenase, glyoxylate reductase, glyoxylate reductase 1, glyoxylate reductase 2, glyoxylate reductase isoform 1, glyoxylate reductase/hydroxypyruvate reductase, glyoxylate/succinic semialdehyde reductase, GLYR1, GLYR2, GOR1, Gor1p, GR/HPR, GR1, GR2, GRHPR, GRHRP, HPR2, HPR3, More, NAD(P)H-dependent GR, NADPH/NADH-dependent glyoxylate/hydroxypyruvate reductases, PfuGRHPR, PhoGRHPR, PtGR, PyaGRHPR, TthGR1
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Cofactor
Cofactor on EC 1.1.1.79 - glyoxylate reductase (NADP+)
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NADH
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enzyme has a higher affinity for NADPH than for NADH when incubated without substrate
NADPH
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enzyme has a higher affinity for NADPH than for NADH when incubated without substrate
NADPH
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preferred cofactor, NADH gives only 4% of the activity with NADPH
NADPH
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preferred cofactor, yields lower Km but similar turnover than NADH
NADPH
glyoxylate reductase 2 uses either NADPH or NADH as a cofactor, however, much greater activity is found with NADPH
NADPH
the highest catalytic efficiency is observed for NADPH
NADPH
the highest catalytic efficiency is observed for NADPH
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comparison of cofactor specificities of various recombinant GRHPR enzymes arising from Pyrococcus furiosus (PfuGRHPR), Pyrococcus horikoshii (PhoGRHPR), and Pyrococcus yayanosii (PyaGRHPR) using glyoxylate or hydroxypyruvate as substrates and NADH or NADPH as cofactors, crystal structures analysis, overview
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additional information
comparison of cofactor specificities of various recombinant GRHPR enzymes arising from Pyrococcus furiosus (PfuGRHPR), Pyrococcus horikoshii (PhoGRHPR), and Pyrococcus yayanosii (PyaGRHPR) using glyoxylate or hydroxypyruvate as substrates and NADH or NADPH as cofactors, crystal structures analysis, overview
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additional information
comparison of cofactor specificities of various recombinant GRHPR enzymes arising from Pyrococcus furiosus (PfuGRHPR), Pyrococcus horikoshii (PhoGRHPR), and Pyrococcus yayanosii (PyaGRHPR) using glyoxylate or hydroxypyruvate as substrates and NADH or NADPH as cofactors, crystal structures analysis, overview
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additional information
recombinant AtGLYR1 prefers NADPH over NADH
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additional information
recombinant AtGLYR1 prefers NADPH over NADH
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additional information
recombinant AtGLYR1 prefers NADPH over NADH
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additional information
recombinant AtGLYR1 prefers NADPH over NADH
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additional information
recombinant AtGLYR2 prefers NADPH over NADH
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additional information
recombinant AtGLYR2 prefers NADPH over NADH
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additional information
recombinant AtGLYR2 prefers NADPH over NADH
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additional information
recombinant AtGLYR2 prefers NADPH over NADH
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additional information
recombinant HPR3 prefers NADPH over NADH
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additional information
recombinant HPR3 prefers NADPH over NADH
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additional information
recombinant HPR3 prefers NADPH over NADH
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additional information
recombinant HPR3 prefers NADPH over NADH
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additional information
the enzyme utilize either NADPH or NADH as the coenzyme with glyoxylate, but prefers NADPH rather than NADH as an electron donor. The coenzyme specificity is provided by a cationic cluster consisting of N184, R185, and N186. Cofactor binding structure, overview
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additional information
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the enzyme utilize either NADPH or NADH as the coenzyme with glyoxylate, but prefers NADPH rather than NADH as an electron donor. The coenzyme specificity is provided by a cationic cluster consisting of N184, R185, and N186. Cofactor binding structure, overview
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additional information
the recombinant AtHPR2 prefers NADPH over NADH
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additional information
the recombinant AtHPR2 prefers NADPH over NADH
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additional information
the recombinant AtHPR2 prefers NADPH over NADH
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additional information
the recombinant AtHPR2 prefers NADPH over NADH
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additional information
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the recombinant AtHPR2 prefers NADPH over NADH
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