Information on EC 1.2.1.72 - erythrose-4-phosphate dehydrogenase

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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
1.2.1.72
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RECOMMENDED NAME
GeneOntology No.
erythrose-4-phosphate dehydrogenase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
D-erythrose 4-phosphate + NAD+ + H2O = 4-phosphoerythronate + NADH + 2 H+
show the reaction diagram
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
oxidation
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redox reaction
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reduction
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
pyridoxal 5'-phosphate biosynthesis I
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vitamin B6 metabolism
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Vitamin B6 metabolism
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Metabolic pathways
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SYSTEMATIC NAME
IUBMB Comments
D-erythrose 4-phosphate:NAD+ oxidoreductase
This enzyme was originally thought to be a glyceraldehyde-3-phosphate dehydrogenase (EC 1.2.1.12), but this has since been disproved, as glyceraldehyde 3-phosphate is not a substrate [1,2]. Forms part of the pyridoxal-5'-phosphate coenzyme biosynthesis pathway in Escherichia coli, along with EC 1.1.1.290 (4-phosphoerythronate dehydrogenase), EC 2.6.1.52 (phosphoserine transaminase), EC 1.1.1.262 (4-hydroxythreonine-4-phosphate dehydrogenase), EC 2.6.99.2 (pyridoxine 5'-phosphate synthase) and EC 1.4.3.5 (pyridoxamine-phosphate oxidase).
CAS REGISTRY NUMBER
COMMENTARY hide
131554-04-6
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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Manually annotated by BRENDA team
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
D-erythrose 4-phosphate + 3-acetylpyridine adenine dinucleotide
4-phosphoerythronate + ?
show the reaction diagram
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?
D-erythrose 4-phosphate + NAD+
4-phosphoerythronate + NADH
show the reaction diagram
D-ribose 5-phosphate + NAD+
? + NADH
show the reaction diagram
D-Ribose 5-phosphate can be used as ketol acceptor substrate in the reaction although D-ribose 5-phosphate is also a substrate for the coupling enzyme
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?
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-erythrose 4-phosphate + NAD+
4-phosphoerythronate + NADH
show the reaction diagram
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the enzyme possible plays a role in the de novo biosynthesis of pyridoxal 5'-phosphate
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?
additional information
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
3-acetylpyridine adenine dinucleotide
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less efficient than NAD+
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
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the enzyme requires the presence of a reducing agent, such as DTT or 2-mercaptoethanol, to maintain activity
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.24 - 1.9
D-erythrose 4-phosphate
0.074 - 5
NAD+
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.21 - 200
D-erythrose 4-phosphate
0.6 - 169
NAD+
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7 - 10
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the pH profile rises steeply between pH 7 and 9 and then drops slightly at pH 10
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
50
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at pH 8.6
PDB
SCOP
CATH
ORGANISM
UNIPROT
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
132000
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gel filtration
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
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x * 37170, mass spectrometry
tetramer
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4 * 37200, SDS-PAGE
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
50
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stable below
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
4C, stable for weeks with negligible loss of activity
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
recombinant
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
C149A
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no significant phosphorylating glyceraldehyde-3-phosphate dehydrogenase activity
C149G
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no significant phosphorylating glyceraldehyde-3-phosphate dehydrogenase activity
C149V
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no significant phosphorylating glyceraldehyde-3-phosphate dehydrogenase activity
C311A
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mutation does not drastically change the phosphorylating glyceraldehyde-3-phosphate dehydrogenase activity. 5.7fold decrease in turnover number for the activity with D-erythrose 4-phosphate and NAD+
C311Y
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mutation does not drastically change the phosphorylating glyceraldehyde-3-phosphate dehydrogenase activity. 33.3fold decrease in turnover number for the activity with D-erythrose 4-phosphate and NAD+
E32D
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mutation does not drastically change the phosphorylating glyceraldehyde-3-phosphate dehydrogenase activity. 2.7fold decrease in turnover number for the activity with D-erythrose 4-phosphate and NAD+
H176N
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turnover number of phosphorylating glyceraldehyde-3-phosphate dehydrogenase activity is decreased by the factor 40. 95.2fold decrease in turnover number for the activity with D-erythrose 4-phosphate and NAD+
M179T
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mutation does not drastically change the phosphorylating glyceraldehyde-3-phosphate dehydrogenase activity. 5fold decrease in turnover number for the activity with D-erythrose 4-phosphate and NAD+
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
degradation
coupling of a transketolase reaction (using Leishmania mexicana transketolase) that converts D-fructose 6-phosphate to D-erythrose 4-phosphate, which can then be converted to 4-phosphate D-erythronate using E4PD, whereby D-ribose 5-phosphate and D-glyceraldehyde 3-phosphate can both be used as ketol acceptor substrates in the reaction
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