Information on EC 1.2.1.89 - D-glyceraldehyde dehydrogenase (NADP+)

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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
1.2.1.89
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RECOMMENDED NAME
GeneOntology No.
D-glyceraldehyde dehydrogenase (NADP+)
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
D-glyceraldehyde + NADP+ + H2O = D-glycerate + NADPH + H+
show the reaction diagram
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
Metabolic pathways
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Microbial metabolism in diverse environments
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Pentose phosphate pathway
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Entner Doudoroff pathway
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SYSTEMATIC NAME
IUBMB Comments
D-glyceraldehyde:NADP+ oxidoreductase
The enzyme from the archaea Thermoplasma acidophilum and Picrophilus torridus is involved in the non-phosphorylative Entner-Doudoroff pathway. cf. EC 1.2.99.8, glyceraldehyde dehydrogenase (FAD-containing).
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
D-glyceraldehyde + NAD+
D-glycerate + NADH + H+
show the reaction diagram
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NAD+ is a very poor cofactor for wild-type
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?
D-glyceraldehyde + NADP+ + H2O
D-glycerate + NADPH + H+
show the reaction diagram
D-glyceraldehyde 3-phosphate + NADP+ + H2O
D-glycerate 3-phosphate + NADPH + H+
show the reaction diagram
glycolaldehyde + NADP+
glycolate + NADPH + H+
show the reaction diagram
additional information
?
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NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
D-glyceraldehyde + NADP+ + H2O
D-glycerate + NADPH + H+
show the reaction diagram
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
NADH
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poor cofoactor
NADP+
NADPH
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NADPH is preferred over NADH
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
Ca2+
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1 mM, 12 h, 4°C, complete loss of activity
Cd2+
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1 mM, 12 h, 4°C, 93% loss of activity
Cu2+
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1 mM, 12 h, 4°C, complete loss of activity
D-glyceraldehyde
slight substrate inhibition, 25% inhibition at 2 mM
Hg2+
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1 mM, 12 h, 4°C, 99% loss of activity
Mg2+
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1 mM, 12 h, 4°C, 24% loss of activity
Mn2+
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1 mM, 12 h, 4°C, 44% loss of activity
Ni2+
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1 mM, 12 h, 4°C, 58% loss of activity
Zn2+
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1 mM, 12 h, 4°C, 46% loss of activity
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2-mercaptoethanol
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1 mM, activity is enhanced more than 2fold
4-chloromercuribenzoic acid
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1 mM, completely inhibits activity
4-hydroxymercuribenzoic acid
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1 mM, completely inhibits activity
DTT
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1 mM, activity is enhanced more than 2fold
glutathione
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1 mM, activity is enhanced more than 2fold
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.06 - 0.33
D-glyceraldehyde
5.1 - 18.3
D-glycerate
11.1 - 12.3
glycolaldehyde
16.7 - 22.7
NAD+
0.017 - 0.42
NADP+
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
10 - 26
D-glyceraldehyde
12 - 20
D-glycerate
20 - 37
glycolaldehyde
1.64 - 10.99
NAD+
10 - 25
NADP+
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
130 - 167
D-glyceraldehyde
639
1.1 - 2.4
D-glycerate
521
1.8 - 3
glycolaldehyde
604
0.07 - 0.63
NAD+
7
24 - 70
NADP+
10
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
2.85
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pH 8.0, 50°C
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4.3 - 8.1
pH 4.3: about 50% of maximal activity, pH 8.1: about 50% of maximal activity
5.8 - 8.7
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pH 5.8: about 50% of maximal activity, pH 8.7: about 50% of maximal activity
6 - 10
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pH 6.0: about 65% of maximal activity, pH 10.0: about 70% of maximal activity
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
30 - 70
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30°C: about 50% of maximal activity, 70°C: about 60% of maximal activity
PDB
SCOP
CATH
ORGANISM
UNIPROT
Thermoplasma acidophilum (strain ATCC 25905 / DSM 1728 / JCM 9062 / NBRC 15155 / AMRC-C165)
Thermoplasma acidophilum (strain ATCC 25905 / DSM 1728 / JCM 9062 / NBRC 15155 / AMRC-C165)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
53000
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4 * 53000, SDS-PAGE
54700
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2 * 54700, calculated from sequence
54782
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4 * 54782, calculated from sequence
55200
2 * 55200, calculated from sequence
115000
gel filtration
120000
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gel filtration
215000
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gel filtration
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
homodimer
homotetramer
tetramer
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6 - 8
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24 h, stable
724216
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
80
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activity is decreased to less than 50% within 20 min
ORGANIC SOLVENT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
guanidine-HCl
isobutanol
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
the gene of TaAlDH is synthesized and cloned into a T7 based vector system for recombinant expression in Escherichia coli. Using matrix-assisted refolding of inclusion bodies the yield of enzyme production is enhanced 43fold
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
F34M/S405N
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enhances enzyme activity with the cofactor NAD+ by a factor of eight
F34M/Y399C/S405N
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enhances enzyme activity with the cofactor NAD+ by a factor of eight and enhances solubilty
Y399C
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enhances the protein solubility after recombinant expression in Escherichia coli 6fold
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
synthesis