1.2.1.79: succinate-semialdehyde dehydrogenase (NADP+)
This is an abbreviated version!
For detailed information about succinate-semialdehyde dehydrogenase (NADP+), go to the full flat file.
Word Map on EC 1.2.1.79
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1.2.1.79
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ssadhs
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nad+
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dehydrogenases
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tricarboxylic
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cyanobacterium
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2-oxoglutarate
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adduct
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moss
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tca
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syntrichia
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shunt
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synechococcus
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medicine
- 1.2.1.79
- ssadhs
- nad+
- dehydrogenases
-
tricarboxylic
- cyanobacterium
- 2-oxoglutarate
- adduct
-
moss
- tca
-
syntrichia
-
shunt
- synechococcus
- medicine
Reaction
Synonyms
AbSSADH, ALDH21, all3556, ApSSADH, gabD, GabD1, NADP+-dependent SSADH, NADP+-dependent succinic semialdehyde dehydrogenase, NADP-dependent succinic semialdehyde dehydrogenase, PpSSALDH, slr0370, Sp2771, SpSSADH, SSADH, SSADH-II, SSALDH, SSO1842, succinic semialdehy de dehydrogenase, succinic semialdehyde dehydrogenase, SYNPCC7002_A2771, SySSADH
ECTree
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Cofactor
Cofactor on EC 1.2.1.79 - succinate-semialdehyde dehydrogenase (NADP+)
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NAD+
NAD+ acts as cosubstrate, but the reaction rates are more than 20fold lower than those with NADP+
NAD+
the enzyme activity in the presence of NADP+ is approximately 20fold higher than that measured in the presence of NAD+
NAD+
kcat/Km for NADP+ is 250fold higher compared to kcat/Km for NAD+
NAD+
preferred cofactor for enzyme mutants S157E and S157P compared to wild-type enzyme
NADP+
electron density analysis of binding site. The enzyme activity measured in the presence of NADP+ is approximately 20fold higher than that measured in the presence of NAD+
NADP+
NAD+ also acts as cosubstrate, but the reaction rates are more than 20fold lower than those with NADP+
NADP+
the enzyme activity in the presence of NADP+ is approximately 20fold higher than that measured in the presence of NAD+
NADP+
kcat/Km for NADP+ is 250fold higher compared to kcat/Km for NAD+
NADP+
enzyme activity increases significantly, and the enzyme becomes resistant to oxidative stress in presence of NADP+ and DTT
NADP+
Ser157 residue in Sp2771 plays a critical structural role in determining NADP+ preference for Sp2771, whereas size and distribution of hydrophobic residues along the substrate binding funnel determine substrate selection
NADP+
preferred cofactor, structural comparison between the apoform and the coenzyme complex reveal that NADP+ binding induces a conformational change of the loop carrying Arg228, which seals the NADP+ in the coenzyme cavity via its 2'-phosphate and alpha-phosphate groups. The presence of a serine residue (Ser197) in PpALDH21 allows for binding of the 2'-phosphate group of NADP+
NADP+
preferred cofactor, the Glu228 residue is located in the NADP+ binding pocket
additional information
no detectable activity by using NAD+ as cofactor
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additional information
AbSSADH can use both NADP+ and NAD+ as electron acceptors but has a greater preference for NADP+. The specific activity of the enzyme with NADP+ is 10times higher than that with NAD+. Residue Ser183 is involved in cofactor binding
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additional information
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AbSSADH can use both NADP+ and NAD+ as electron acceptors but has a greater preference for NADP+. The specific activity of the enzyme with NADP+ is 10times higher than that with NAD+. Residue Ser183 is involved in cofactor binding
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additional information
ApSSADH prefers to use NADP+ rather than NAD+ as its cofactor. Residue Ser157 of ApSSADH plays a critical role in determining the cofactor preference. The catalytic activities of mutants S157E and S157P are elevated when the cofactor is switched from NADP+ to NAD+
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additional information
NAD+ is a very poor coenzyme for ALDH21, the activity with NAD+ is only about 3% of that with NADP+
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additional information
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NAD+ is a very poor coenzyme for ALDH21, the activity with NAD+ is only about 3% of that with NADP+
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