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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Subunits
Subunits on EC 1.2.1.79 - succinate-semialdehyde dehydrogenase (NADP+)
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dimer
homodimer
tetramer
additional information
the central parts of both cofactor binding domain and catalytic domain contain atypical alpha/beta structure. The catalytic domain consists of a seven stranded beta-sheet flanked by two alpha-helices on one side and three alpha-helices on the other side.The cofactor binding domain displays the two tandem Rossmann folds for NADP+ binding . The oligomerization domain contains three-stranded antiparallel beta-sheets protruding across the center of the dimer interface, while the NADP+ binding site is on the opposite side of the dimer interface
2 * 50000, recombinant His-tagged enzyme, SDS-PAGE, 2 * 50985, His-tagged enzyme, sequence calculation, 2 * 50853, recombinant enzyme, mass spectrometry
dimer
Sp2771 monomer is composed of N-terminal cofactor binding domain, a catalytic domain and an oligomerization domain
homodimer
gel filtration, SySSADH monomer consists of three segments - alpha/beta-fold N- and C-domains for a cofactor binding and a catalytic domain, and three antiparallel beta-strands constituting a dimerization domain
homodimer
the overall structure of monomeric SySSADH is reminiscent of an ALDH fold. It is made up of three segments: alpha/beta-fold N- and C-domains for a cofactor binding and a catalytic domain, respectively, and three antiparallel beta-strands constituting a dimerization domain
homodimer
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the overall structure of monomeric SySSADH is reminiscent of an ALDH fold. It is made up of three segments: alpha/beta-fold N- and C-domains for a cofactor binding and a catalytic domain, respectively, and three antiparallel beta-strands constituting a dimerization domain
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