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Literature summary for 1.2.1.79 extracted from

  • Kopecna, M.; Vigouroux, A.; Vilim, J.; Koncitikova, R.; Briozzo, P.; Hajkova, E.; Jaskova, L.; von Schwartzenberg, K.; Sebela, M.; Morera, S.; Kopecny, D.
    The ALDH21 gene found in lower plants and some vascular plants codes for a NADP+-dependent succinic semialdehyde dehydrogenase (2017), Plant J., 92, 229-243 .
    View publication on PubMed

Crystallization (Commentary)

Crystallization (Comment) Organism
purified PpALDH21 in apoform, and in complex with succinate and NADP+, X-ray diffraction structure determination and analysis at 2.15-2.30 A resolution, structure modeling Physcomitrium patens

Protein Variants

Protein Variants Comment Organism
N175A site-directed mutagenesis, the mutant shows reduced activity compared tow wild-type enzyme Physcomitrium patens
R121A site-directed mutagenesis, almost inactive mutant Physcomitrium patens
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 Physcomitrium patens
R457A site-directed mutagenesis, almost inactive mutant Physcomitrium patens
Y296A site-directed mutagenesis, the mutant shows reduced activity compared tow wild-type enzyme Physcomitrium patens

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.024
-
NADP+ recombinant wild-type enzyme, pH 8.2, 25°C, with succinate semialdehyde Physcomitrium patens
0.127
-
succinate semialdehyde recombinant mutant R228A, pH 8.2, 25°C, with NADP+ Physcomitrium patens
0.127
-
succinate semialdehyde recombinant mutant Y296A, pH 8.2, 25°C, with NADP+ Physcomitrium patens
0.135
-
succinate semialdehyde recombinant mutant R457A, pH 8.2, 25°C, with NADP+ Physcomitrium patens
0.181
-
succinate semialdehyde recombinant wild-type enzyme, pH 8.2, 25°C, with NADP+ Physcomitrium patens
0.268
-
succinate semialdehyde recombinant mutant R121A, pH 8.2, 25°C, with NADP+ Physcomitrium patens
0.375
-
NADP+ recombinant mutant R228A, pH 8.2, 25°C, with succinate semialdehyde Physcomitrium patens
0.551
-
Glutaric semialdehyde recombinant wild-type enzyme, pH 8.2, 25°C, with NADP+ Physcomitrium patens
1.49
-
succinate semialdehyde recombinant mutant N175A, pH 8.2, 25°C, with NADP+ Physcomitrium patens
5.37
-
NAD+ recombinant wild-type enzyme, pH 8.2, 25°C, with succinate semialdehyde Physcomitrium patens
8.44
-
NAD+ recombinant mutant R228A, pH 8.2, 25°C, with succinate semialdehyde Physcomitrium patens

Localization

Localization Comment Organism GeneOntology No. Textmining
cytosol
-
Physcomitrium patens 5829
-

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
succinate semialdehyde + NADP+ + H2O Physcomitrium patens
-
succinate + NADPH + 2 H+
-
?

Organism

Organism UniProt Comment Textmining
Physcomitrium patens A9SS48
-
-

Reaction

Reaction Comment Organism Reaction ID
succinate semialdehyde + NADP+ + H2O = succinate + NADPH + 2 H+ two arginine residues at positions 121 and 457 are both essential for the catalytic activity of ALDH21 and for the binding of SSAL Physcomitrium patens

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
glutaric semialdehyde + NADP+ + H2O
-
Physcomitrium patens glutarate + NADPH + 2 H+
-
?
additional information glutaric semialdehyde (GRSAL) is the second-best substrate, but it is oxidized at only 1.2% rate compared with succinate semialdehyde Physcomitrium patens ?
-
-
succinate semialdehyde + NAD+ + H2O poor cofactor for the wild-type enzyme, but is utilized by enzyme mutants, overview Physcomitrium patens succinate + NADH + 2 H+
-
?
succinate semialdehyde + NADP+ + H2O
-
Physcomitrium patens succinate + NADPH + 2 H+
-
?
succinate semialdehyde + NADP+ + H2O specific for Physcomitrium patens succinate + NADPH + 2 H+
-
?

Subunits

Subunits Comment Organism
tetramer
-
Physcomitrium patens

Synonyms

Synonyms Comment Organism
ALDH21
-
Physcomitrium patens
NADP+-dependent succinic semialdehyde dehydrogenase
-
Physcomitrium patens
PpSSALDH
-
Physcomitrium patens
SSALDH
-
Physcomitrium patens

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
25
-
assay at Physcomitrium patens

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
0.02
-
succinate semialdehyde recombinant mutant R121A, pH 8.2, 25°C, with NADP+ Physcomitrium patens
0.02
-
succinate semialdehyde recombinant mutant R457A, pH 8.2, 25°C, with NADP+ Physcomitrium patens
0.27
-
Glutaric semialdehyde recombinant wild-type enzyme, pH 8.2, 25°C, with NADP+ Physcomitrium patens
1.2
-
NAD+ recombinant mutant R228A, pH 8.2, 25°C, with succinate semialdehyde Physcomitrium patens
3.3
-
NAD+ recombinant wild-type enzyme, pH 8.2, 25°C, with succinate semialdehyde Physcomitrium patens
5.7
-
succinate semialdehyde recombinant mutant R228A, pH 8.2, 25°C, with NADP+ Physcomitrium patens
6.4
-
NADP+ recombinant mutant R228A, pH 8.2, 25°C, with succinate semialdehyde Physcomitrium patens
7.1
-
succinate semialdehyde recombinant mutant Y296A, pH 8.2, 25°C, with NADP+ Physcomitrium patens
12.5
-
succinate semialdehyde recombinant mutant N175A, pH 8.2, 25°C, with NADP+ Physcomitrium patens
15.2
-
NADP+ recombinant wild-type enzyme, pH 8.2, 25°C, with succinate semialdehyde Physcomitrium patens
15.8
-
succinate semialdehyde recombinant wild-type enzyme, pH 8.2, 25°C, with NADP+ Physcomitrium patens

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
8.2
-
with cofactor NADP+ Physcomitrium patens

pH Range

pH Minimum pH Maximum Comment Organism
6 9.5 50% of maximal activity within this range, pH-profile overview Physcomitrium patens

Cofactor

Cofactor Comment Organism Structure
additional information NAD+ is a very poor coenzyme for ALDH21, the activity with NAD+ is only about 3% of that with NADP+ Physcomitrium patens
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+ Physcomitrium patens

General Information

General Information Comment Organism
malfunction both R121A and R457A variants are almost inactive, demonstrating a key role of each arginine in catalysis Physcomitrium patens
metabolism the enzyme is involved in the GABA shunt pathway, GABA shunt reactions from glutamate to succinate might appear in cytosol in addition to mitochondria making the GABA shunt pathway much more diverse Physcomitrium patens
additional information the crystal structure with the bound product succinate shows that its carboxylate group establishes salt bridges with both Arg121 and Arg457, and a hydrogen bond with Tyr296. While both arginine residues are pre-formed for substrate/product binding, Tyr296 moves by more than 1.0 A. Key role of R121 and R457 residues in catalysis. Structure-function analysis, overview Physcomitrium patens
physiological function ALDH21 from the moss Physcomitrella patens codes for a tetrameric NADP+-dependent succinic semialdehyde dehydrogenase (SSALDH), which converts succinate semialdehyde, an intermediate of the gamma-aminobutyric acid (GABA) shunt pathway, into succinate in the cytosol Physcomitrium patens

kcat/KM [mM/s]

kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
0.075
-
succinate semialdehyde recombinant mutant R121A, pH 8.2, 25°C, with NADP+ Physcomitrium patens
0.142
-
NAD+ recombinant mutant R228A, pH 8.2, 25°C, with succinate semialdehyde Physcomitrium patens
0.148
-
succinate semialdehyde recombinant mutant R457A, pH 8.2, 25°C, with NADP+ Physcomitrium patens
0.49
-
Glutaric semialdehyde recombinant wild-type enzyme, pH 8.2, 25°C, with NADP+ Physcomitrium patens
0.615
-
NAD+ recombinant wild-type enzyme, pH 8.2, 25°C, with succinate semialdehyde Physcomitrium patens
8.39
-
succinate semialdehyde recombinant mutant N175A, pH 8.2, 25°C, with NADP+ Physcomitrium patens
17.07
-
NADP+ recombinant mutant R228A, pH 8.2, 25°C, with succinate semialdehyde Physcomitrium patens
44.88
-
succinate semialdehyde recombinant mutant R228A, pH 8.2, 25°C, with NADP+ Physcomitrium patens
55.91
-
succinate semialdehyde recombinant mutant Y296A, pH 8.2, 25°C, with NADP+ Physcomitrium patens
87.29
-
succinate semialdehyde recombinant wild-type enzyme, pH 8.2, 25°C, with NADP+ Physcomitrium patens
633.3
-
NADP+ recombinant wild-type enzyme, pH 8.2, 25°C, with succinate semialdehyde Physcomitrium patens