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Information on EC 1.2.1.72 - erythrose-4-phosphate dehydrogenase and Organism(s) Escherichia coli and UniProt Accession P0A9B6
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1.2.1.72 erythrose-4-phosphate dehydrogenaseIUBMB Comments
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).
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The taxonomic range for the selected organisms is: Escherichia coli
The enzyme appears in selected viruses and cellular organisms
The enzyme appears in selected viruses and cellular organisms
Synonyms
gapb-encoded protein, e4pdh, erythrose-4-phosphate dehydrogenase, erythrose 4-phosphate dehydrogenase, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
GapB
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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
131554-04-6
-
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
D-erythrose 4-phosphate + NAD+
4-phosphoerythronate + NADH
production of E4P can be coupled to the NADH generating E4PD activity which enables measurement of the transketolase reaction involving F6P as donor substrate
-
-
?
D-ribose 5-phosphate + NAD+
? + NADH
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
-
-
?
D-erythrose 4-phosphate + 3-acetylpyridine adenine dinucleotide
4-phosphoerythronate + ?
-
-
-
-
?
D-erythrose 4-phosphate + NAD+
4-phosphoerythronate + NADH
-
the enzyme possible plays a role in the de novo biosynthesis of pyridoxal 5'-phosphate
-
-
?
D-erythrose 4-phosphate + NAD+
4-phosphoerythronate + NADH
-
the chemical mechanism of erythrose 4-phosphate oxidation by gap-encoded protein proceeds through a two-step mechanism involving covalent intermediates with Cys149, with rates associated to the acylation and deacylation process of 280 per s and 20 per s, respectively. No isotopic solvent effect is observed, suggesting that the rate-limiting step is not hydrolysis
-
-
?
additional information
?
-
fructose 6-phosphate, glycerol 6-phosphate and glyceraldehyde 3-phosphate can not be used as substrate by E4PD when added up to 50 mM
-
-
?
additional information
?
-
-
enzyme is involved in pyridoxal 5'-phosphate coenzyme biosynthesis in Escherichia coli K-12
-
-
?
additional information
?
-
-
epd expression is very low in Escherichia coli. In presence of glucose, the 3 epd, pgk and fba ORFs are efficiently cotranscribed from promoter epd P0. Translational limitation of the epd expression in Escherichia coli
-
-
?
additional information
?
-
-
gapB is dispensable for glycolysis and pyridoxal biosynthesis pathway
-
-
?
additional information
?
-
-
the enzyme also shows low phosphorylating glyceraldehyde-3-phosphate dehydrogenase activity
-
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
D-erythrose 4-phosphate + NAD+
4-phosphoerythronate + NADH
-
the enzyme possible plays a role in the de novo biosynthesis of pyridoxal 5'-phosphate
-
-
?
additional information
?
-
-
enzyme is involved in pyridoxal 5'-phosphate coenzyme biosynthesis in Escherichia coli K-12
-
-
?
additional information
?
-
-
epd expression is very low in Escherichia coli. In presence of glucose, the 3 epd, pgk and fba ORFs are efficiently cotranscribed from promoter epd P0. Translational limitation of the epd expression in Escherichia coli
-
-
?
additional information
?
-
-
gapB is dispensable for glycolysis and pyridoxal biosynthesis pathway
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
-
the enzyme requires the presence of a reducing agent, such as DTT or 2-mercaptoethanol, to maintain activity
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7 - 10
-
the pH profile rises steeply between pH 7 and 9 and then drops slightly at pH 10
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
C149A
-
no significant phosphorylating glyceraldehyde-3-phosphate dehydrogenase activity
C149G
-
no significant phosphorylating glyceraldehyde-3-phosphate dehydrogenase activity
C149V
-
no significant phosphorylating glyceraldehyde-3-phosphate dehydrogenase activity
C311A
-
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
-
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
-
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
-
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
-
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+
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
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
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Zhao, G.; Pease, A.J.; Bharani, N.; Winkler, M.E.
Biochemical characterization of gapB-encoded erythrose 4-phosphate dehydrogenase of Escherichia coli K-12 and its possible role in pyridoxal 5'-phosphate biosynthesis
J. Bacteriol.
177
2804-2812
1995
Escherichia coli
Seta, F.D.; Boschi-Muller, S.; Vignais, M.L.; Branlant, G.
Characterization of Escherichia coli strains with gapA and gapB genes deleted
J. Bacteriol.
179
5218-5221
1997
Escherichia coli
Yang, Y.; Zhao, G.; Man, T.K.; Winkler, M.E.
Involvement of the gapA- and epd (gapB)-encoded dehydrogenases in pyridoxal 5'-phosphate coenzyme biosynthesis in Escherichia coli K-12
J. Bacteriol.
180
4294-4299
1998
Escherichia coli
Boschi-Muller, S.; Azza, S.; Pollastro, D.; Corbier, C.; Branlant, G.
Comparative enzymatic properties of GapB-encoded erythrose-4-phosphate dehydrogenase of Escherichia coli and phosphorylating glyceraldehyde-3-phosphate dehydrogenase
J. Biol. Chem.
272
15106-15112
1997
Escherichia coli
Bardey, V.; Vallet, C.; Robas, N.; Charpentier, B.; Thouvenot, B.; Mougin, A.; Hajnsdorf, E.; Regnier, P.; Springer, M.; Branlant, C.
Characterization of the molecular mechanisms involved in the differential production of erythrose-4-phosphate dehydrogenase, 3-phosphoglycerate kinase and class II fructose-1,6-bisphosphate aldolase in Escherichia coli
Mol. Microbiol.
57
1265-1287
2005
Escherichia coli
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