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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

Reaction

succinate semialdehyde
+
NADP+
+
H2O
=
succinate
+
NADPH
+ 2 H+

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

     1 Oxidoreductases
         1.2 Acting on the aldehyde or oxo group of donors
             1.2.1 With NAD+ or NADP+ as acceptor
                1.2.1.79 succinate-semialdehyde dehydrogenase (NADP+)

Engineering

Engineering on EC 1.2.1.79 - succinate-semialdehyde dehydrogenase (NADP+)

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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
C289A
site-directed mutagenesis, inactive mutant
C291A
site-directed mutagenesis, the mutant shows 65% activity compared to wild-type enzyme
E228A
site-directed mutagenesis, inactive mutant
E228D
sitedirected mutagenesis, the mutant shows highly reduced activity compared to wild-type enzyme
N131A
site-directed mutagenesis, inactive mutant
N131D
site-directed mutagenesis, inactive mutant
R139A
site-directed mutagenesis, the mutant displays catalytic efficiency (kcat/Km) of only respective 0.2% compared to wild-type enzyme with significantly decreased binding affinity for succinic semialdehyde
S157E
site-directed mutagenesis, the mutant shows altered cofactor specificity compared to wild-type, preferring NAD+, mutation of Ser157 does not significantly affect the binding affinity of SSA with the enzyme
S157P
site-directed mutagenesis, the mutant shows altered cofactor specificity compared to wild-type, preferring NAD+, mutation of Ser157 does not significantly affect the binding affinity of SSA with the enzyme
S420A
site-directed mutagenesis, the mutant displays catalytic efficiency (kcat/Km) of only respective 0.4% compared to wild-type enzyme with significantly decreased binding affinity for succinic semialdehyde
N175A
site-directed mutagenesis, the mutant shows reduced activity compared tow wild-type enzyme
R121A
site-directed mutagenesis, almost inactive mutant
R228A
site-directed mutagenesis, the mutation results in 37fold lower catalytic efficiency value (kcat/Km) for NADP+, but only fourfold lower value for NAD+ compared to wild-type
R457A
site-directed mutagenesis, almost inactive mutant
Y296A
site-directed mutagenesis, the mutant shows reduced activity compared tow wild-type enzyme
C262A
E228A
E228Q
active site mutation, nonfunctional because Glu-228 acts as a general base
F132A
activity of about 10–30% of the wild type enzyme, indicating a contribution of these succinic semialdehyde binding residues to the overall enzyme activity
F425A
inactive, suggesting that Phe-425 plays an important role in substrate binding
I263A
activity of about 10–30% of the wild type enzyme, indicating a contribution of these succinic semialdehyde binding residues to the overall enzyme activity
N131A
mutation of a residue that interacts with the O4 atom or the carboxyl group of succinic semialdehyde thus abolishing enzyme activity
N131D
mutation of a residue that interacts with the O4 atom or the carboxyl group of succinic semialdehyde thus abolishing enzyme activity
R139A
R139K
mutant enzyme exhibited an activity up to 80% that of the wild type enzyme, suggesting the significance of a positively charged residue in the binding of the carboxyl group of succinic semialdehyde
S157E
mutation changes cofactor preference from NADP+ to NAD+, but enzyme activity is approximately 10fold reduced
S419A
W135A
activity of about 10–30% of the wild type enzyme, indicating a contribution of these succinic semialdehyde binding residues to the overall enzyme activity
C262A
site-directed mutagenesis, Sp2771 mutant structure analysis and comparison to the wild-type structure
S419A
site-directed mutagenesis, Sp2771 mutant structure analysis and comparison to the wild-type structure
additional information
metabolic engineering of Corynebacterium glutamicum for the production of glutaric acid, a C5 dicarboxylic acid platform chemical, by co-expression of Pseudomonas putida davT, davB, and davD genes encoding lysine 2-monooxygenase, delta-aminovaleramidase, and glutarate semialdehyde dehydrogenase, respectively, in Corynebacterium glutamicum. Method optimization and evaluation. The glutaric acid biosynthesis pathway constructed in recombinant Corynebacterium glutamicum is engineered by examining strong synthetic promoters H30 and H36, Corynebacterium glutamicum codon-optimized davTDBA genes, and modification of davB gene with an N-terminal His6-tag to improve the production of glutaric acid. The use of N-terminal His6-tagged DavB is most suitable for the production of glutaric acid from glucose. Fed-batch fermentation of the final engineered Corynebacterium glutamicum H30_GAHis strain, expressing davTDA genes along with davB fused with His6-tag at N-terminus can produce 24.5 g/l of glutaric acid with low accumulation of L-lysine (1.7 g/l), wherein 5-aminovaleric acid (5-AVA) ccumulation is not observed during fermentation. Metabolically engineered Corynebacterium glutamicum strain KCTC H30_GA-2 (engineered strain KCTC 1857) is able for catalysis of the biosynthesis of glutaric acid from glucose. Method optimization and evaluation, overview