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

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The expected taxonomic range for this enzyme is: Bacteria, Archaea

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
Entner Doudoroff pathway
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Pentose phosphate pathway
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Metabolic pathways
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Microbial metabolism in diverse environments
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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
cf. EC 1.2.1.22
SwissProt
Manually annotated by BRENDA team
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 + NAD+ + H2O
D-glycerate + NADH + H+
show the reaction diagram
activity of mutants N286E, N286H, N286T. No substrate 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
glyceraldehyde + NAD+ + H2O
glycerate + NADH + H+
show the reaction diagram
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?
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 - 2.2
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 - 957
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
31.64 - 485.8
D-glyceraldehyde
1.1 - 2.4
D-glycerate
1.8 - 3
glycolaldehyde
0.07 - 0.63
NAD+
24 - 70
NADP+
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.08
mutant N286H, pH 7.0, 37°C
0.13
mutant N286H, pH 7.0, 37°C
1.1
mutant N286H, pH 7.0, 37°C
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
?
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x * 55000, SDS-PAGE
homodimer
homotetramer
tetramer
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
structures of wild-type and mutant F34M/S405N, to 1.95 A resolution for wild-type and 2.14 and 2.10 A resolution for the mutant
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pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6 - 8
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24 h, stable
724216
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
55
1 h, 70% residual activity for mutant N286T
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
HiTrap column chromatography
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
; expressed in Escherichia coli BL21(DE3) cells
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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
N286E
engineering of L-lactaldehyde dehydrogenase. Contrary to wild-type, mutant is able to oxidate glyceraldehyde
N286H
engineering of L-lactaldehyde dehydrogenase. Contrary to wild-type, mutant is able to oxidate glyceraldehyde
N286T
engineering of L-lactaldehyde dehydrogenase. Contrary to wild-type, mutant is able to oxidate glyceraldehyde. Compared to L-lactaldehyde, N286T has a one-third lower Km value to glyceraldehyde.
34M/Y399C/S405N
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the mutations enhance enzyme activity with the cofactor NAD+ by a factor of 55.7
F34L
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the mutation enhances enzyme activity with the cofactor NAD+ by a factor of 3.2
F34M/D372N/S405N
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the mutations enhance enzyme activity with the cofactor NAD+ by a factor of 7.2
F34M/D372N/Y399C/S405N
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the mutations enhance enzyme activity with the cofactor NAD+ by a factor of 35.1
F34M/S405N
F34M/W271R/S405N
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the mutations enhance enzyme activity with the cofactor NAD+ by a factor of 22.6
F34M/W271S/S405N
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the mutations enhance enzyme activity with the cofactor NAD+ by a factor of 42.5
F34M/W271S/Y399C/S405N
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the mutations enhance enzyme activity with the cofactor NAD+ by a factor of 1.1
F34M/Y399C/S405N
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enhances enzyme activity with the cofactor NAD+ by a factor of eight and enhances solubilty
S405C
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the mutation enhances enzyme activity with the cofactor NAD+ by a factor of 6
S405N
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the mutation enhances enzyme activity with the cofactor NAD+ by a factor of 7.4
W271S
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the mutations enhance enzyme activity with the cofactor NAD+ by a factor of 17.1
Y399C
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enhances the protein solubility after recombinant expression in Escherichia coli 6fold; the mutation enhances the protein solubility after recombinant expression in Escherichia coli 6fold and enhances enzyme activity with the cofactor NAD+ by a factor of 6.4
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
synthesis