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Literature summary for 1.2.1.90 extracted from

  • Corregido, M.; Asencion Diez, M.; Iglesias, A.; Piattoni, C.
    New pieces to the carbon metabolism puzzle of Nitrosomonas europaea kinetic characterization of glyceraldehyde-3 phosphate and succinate semialdehyde dehydrogenases (2019), Biochimie, 158, 238-245 .
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
gene gapD, DNA and amino acid sequence determination and analysis, sequence comparisons, recombinant expression of N-terminally His-tagged enzyme in Escherichia coli strain BL21(DE3) Nitrosomonas europaea

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.23
-
NADP+ pH 8.5, 30°C, recombinant enzyme, with succinate semialdehyde Nitrosomonas europaea
0.4
-
NAD+ pH 8.5, 30°C, recombinant enzyme, with succinate semialdehyde Nitrosomonas europaea
1.9
-
D-glyceraldehyde 3-phosphate pH 8.5, 30°C, recombinant enzyme, with NADP+ Nitrosomonas europaea
2.2
-
D-glyceraldehyde 3-phosphate pH 8.5, 30°C, recombinant enzyme, with NAD+ Nitrosomonas europaea
3
-
L-Glyceraldehyde 3-phosphate about, pH 8.5, 30°C, recombinant enzyme, with NADP+ Nitrosomonas europaea

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
D-glyceraldehyde 3-phosphate + NAD+ + H2O Nitrosomonas europaea
-
3-phospho-D-glycerate + NADH + 2 H+
-
ir
D-glyceraldehyde 3-phosphate + NADP+ + H2O Nitrosomonas europaea
-
3-phospho-D-glycerate + NADPH + 2 H+
-
ir

Organism

Organism UniProt Comment Textmining
Nitrosomonas europaea Q82TA7 cf. EC 1.2.1.16
-
Nitrosomonas europaea ATCC 19718 Q82TA7 cf. EC 1.2.1.16
-
Nitrosomonas europaea CIP 103999 Q82TA7 cf. EC 1.2.1.16
-
Nitrosomonas europaea KCTC 2705 Q82TA7 cf. EC 1.2.1.16
-
Nitrosomonas europaea NBRC 14298 Q82TA7 cf. EC 1.2.1.16
-

Purification (Commentary)

Purification (Comment) Organism
recombinant His-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography and dialysis Nitrosomonas europaea

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
D-glyceraldehyde 3-phosphate + NAD+ + H2O
-
Nitrosomonas europaea 3-phospho-D-glycerate + NADH + 2 H+
-
ir
D-glyceraldehyde 3-phosphate + NADP+ + H2O
-
Nitrosomonas europaea 3-phospho-D-glycerate + NADPH + 2 H+
-
ir
L-glyceraldehyde 3-phosphate + NAD+ + H2O
-
Nitrosomonas europaea 3-phospho-L-glycerate + NADH + 2 H+
-
ir
L-glyceraldehyde 3-phosphate + NADP+ + H2O
-
Nitrosomonas europaea 3-phospho-L-glycerate + NADPH + 2 H+
-
ir
additional information the enzyme is also active with succinate semialdehyde (SSA), cf. EC 1.2.1.16. Values obtained reflect a 3500 and 87fold higher catalytic efficiency when SSA/NADP+ or SSA/NAD+ pairs, respectively, are used instead of Ga3P/NADP+ or Ga3P/NAD+. When D-Ga3P is the substrate, no significant differences for NADP+ or NAD+ are observed. In addition, recombinant GabD is able to oxidize both D- and L-Ga3P isomers with either NADP+ or NAD+ as cofactors with similar apparent Km values for D- or L-Ga3P and twice the kcat with D-Ga3P with both cofactors. No activity with formaldehyde, glutaraldehyde, ethanol, and glycerol as substrates Nitrosomonas europaea ?
-
-
additional information the enzyme is also active with succinate semialdehyde (SSA), cf. EC 1.2.1.16. Values obtained reflect a 3500 and 87fold higher catalytic efficiency when SSA/NADP+ or SSA/NAD+ pairs, respectively, are used instead of Ga3P/NADP+ or Ga3P/NAD+. When D-Ga3P is the substrate, no significant differences for NADP+ or NAD+ are observed. In addition, recombinant GabD is able to oxidize both D- and L-Ga3P isomers with either NADP+ or NAD+ as cofactors with similar apparent Km values for D- or L-Ga3P and twice the kcat with D-Ga3P with both cofactors. No activity with formaldehyde, glutaraldehyde, ethanol, and glycerol as substrates Nitrosomonas europaea NBRC 14298 ?
-
-
additional information the enzyme is also active with succinate semialdehyde (SSA), cf. EC 1.2.1.16. Values obtained reflect a 3500 and 87fold higher catalytic efficiency when SSA/NADP+ or SSA/NAD+ pairs, respectively, are used instead of Ga3P/NADP+ or Ga3P/NAD+. When D-Ga3P is the substrate, no significant differences for NADP+ or NAD+ are observed. In addition, recombinant GabD is able to oxidize both D- and L-Ga3P isomers with either NADP+ or NAD+ as cofactors with similar apparent Km values for D- or L-Ga3P and twice the kcat with D-Ga3P with both cofactors. No activity with formaldehyde, glutaraldehyde, ethanol, and glycerol as substrates Nitrosomonas europaea ATCC 19718 ?
-
-
additional information the enzyme is also active with succinate semialdehyde (SSA), cf. EC 1.2.1.16. Values obtained reflect a 3500 and 87fold higher catalytic efficiency when SSA/NADP+ or SSA/NAD+ pairs, respectively, are used instead of Ga3P/NADP+ or Ga3P/NAD+. When D-Ga3P is the substrate, no significant differences for NADP+ or NAD+ are observed. In addition, recombinant GabD is able to oxidize both D- and L-Ga3P isomers with either NADP+ or NAD+ as cofactors with similar apparent Km values for D- or L-Ga3P and twice the kcat with D-Ga3P with both cofactors. No activity with formaldehyde, glutaraldehyde, ethanol, and glycerol as substrates Nitrosomonas europaea KCTC 2705 ?
-
-
additional information the enzyme is also active with succinate semialdehyde (SSA), cf. EC 1.2.1.16. Values obtained reflect a 3500 and 87fold higher catalytic efficiency when SSA/NADP+ or SSA/NAD+ pairs, respectively, are used instead of Ga3P/NADP+ or Ga3P/NAD+. When D-Ga3P is the substrate, no significant differences for NADP+ or NAD+ are observed. In addition, recombinant GabD is able to oxidize both D- and L-Ga3P isomers with either NADP+ or NAD+ as cofactors with similar apparent Km values for D- or L-Ga3P and twice the kcat with D-Ga3P with both cofactors. No activity with formaldehyde, glutaraldehyde, ethanol, and glycerol as substrates Nitrosomonas europaea CIP 103999 ?
-
-

Synonyms

Synonyms Comment Organism
More see also EC 1.2.1.16 Nitrosomonas europaea
non-phosphorylating Ga3PDHase
-
Nitrosomonas europaea

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
30
-
assay at Nitrosomonas europaea

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
0.007
-
L-Glyceraldehyde 3-phosphate about, pH 8.5, 30°C, recombinant enzyme Nitrosomonas europaea
0.0133
-
D-glyceraldehyde 3-phosphate pH 8.5, 30°C, recombinant enzyme, with NADP+ Nitrosomonas europaea
0.0133
-
NADP+ pH 8.5, 30°C, recombinant enzyme, with succinate semialdehyde Nitrosomonas europaea
0.0167
-
D-glyceraldehyde 3-phosphate pH 8.5, 30°C, recombinant enzyme, with NAD+ Nitrosomonas europaea
0.0167
-
NAD+ pH 8.5, 30°C, recombinant enzyme, with succinate semialdehyde Nitrosomonas europaea

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
8.5
-
assay at Nitrosomonas europaea

Cofactor

Cofactor Comment Organism Structure
additional information when D-Ga3P is the substrate, no significant differences for NADP+ or NAD+ are observed Nitrosomonas europaea
NAD+
-
Nitrosomonas europaea
NADP+
-
Nitrosomonas europaea

General Information

General Information Comment Organism
physiological function enzyme GabD irreversibly oxidizes D-glyceraldehyde 3-phosphate (Ga3P) to 3-phospho-D-glycerate (3Pglycerate) using NAD+ or NADP+, thus resembling a non-phosphorylating Ga3PDHase. But the enzyme shows about 6fold higher Km value and three orders of magnitude higher catalytic efficiency with succinate semialdehyde (SSA) and NADP+. Indeed, the GabD protein identity corresponds to an SSA dehydrogenase (SSADHase, EC 1.2.1.16) Nitrosomonas europaea

kcat/KM [mM/s]

kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
0.0023
-
L-Glyceraldehyde 3-phosphate about, pH 8.5, 30°C, recombinant enzyme, with NADP+ Nitrosomonas europaea
0.007
-
D-glyceraldehyde 3-phosphate pH 8.5, 30°C, recombinant enzyme, with NADP+ Nitrosomonas europaea
0.0076
-
D-glyceraldehyde 3-phosphate pH 8.5, 30°C, recombinant enzyme, with NAD+ Nitrosomonas europaea
0.0418
-
NAD+ pH 8.5, 30°C, recombinant enzyme, with succinate semialdehyde Nitrosomonas europaea
0.0578
-
NADP+ pH 8.5, 30°C, recombinant enzyme, with succinate semialdehyde Nitrosomonas europaea