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Information on EC 4.1.2.20 - 2-dehydro-3-deoxyglucarate aldolase and Organism(s) Escherichia coli and UniProt Accession P23522

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EC Tree
     4 Lyases
         4.1 Carbon-carbon lyases
             4.1.2 Aldehyde-lyases
                4.1.2.20 2-dehydro-3-deoxyglucarate aldolase
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This record set is specific for:
Escherichia coli
UNIPROT: P23522 not found.
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Word Map
The taxonomic range for the selected organisms is: Escherichia coli
The expected taxonomic range for this enzyme is: Bacteria, Archaea, Eukaryota
Synonyms
kdg aldolase, ddg aldolase, 2-dehydro-3-deoxygalactarate aldolase, 2-keto-3-deoxy gluconate aldolase, 5-keto-4-deoxy-(d)-glucarate aldolase, 5-keto-4-deoxy-d-glucarate aldolase, 4-hydroxy-2-ketoheptane-1,7-dioate aldolase, kdg-specific aldolase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4-hydroxy-2-ketoheptane-1,7-dioate aldolase
-
2-dehydro-3-deoxygalactarate aldolase
-
-
-
-
2-keto-3-deoxy gluconate aldolase
-
2-keto-3-deoxy-glucarate aldolase
-
-
-
-
2-keto-3-deoxyglucarate aldolase
-
-
-
-
5-KDGluc aldolase
-
-
-
-
5-Keto-4-deoxy-(D)-glucarate aldolase
-
-
-
-
5-keto-4-deoxy-D-glucarate aldolase
-
-
-
-
aldolase, 2-keto-3-deoxy-D-glucarate
-
-
-
-
DDG aldolase
-
-
-
-
KDG aldolase
-
KDGLucA
-
-
-
-
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
2-dehydro-3-deoxy-D-glucarate = pyruvate + 2-hydroxy-3-oxopropanoate
show the reaction diagram
mechanism
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
PATHWAY SOURCE
PATHWAYS
-
-, -
SYSTEMATIC NAME
IUBMB Comments
2-dehydro-3-deoxy-D-glucarate tartronate-semialdehyde-lyase (pyruvate-forming)
-
CAS REGISTRY NUMBER
COMMENTARY hide
37290-56-5
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
2-dehydro-3-deoxy-L-rhamnonate
?
show the reaction diagram
-
-
-
?
2-keto-3-deoxy-L-lyxonate
?
show the reaction diagram
-
-
-
?
2-keto-3-deoxy-L-mannonate
?
show the reaction diagram
-
-
-
?
4-hydroxy-2-ketoheptane-1,7-dioate
pyruvate + succinic semialdehyde
show the reaction diagram
-
-
-
?
4-hydroxy-2-ketohexanoic acid
?
show the reaction diagram
-
-
-
?
4-hydroxy-2-ketopentanoic acid
?
show the reaction diagram
-
-
-
?
2-dehydro-3-deoxy-D-galactonate
?
show the reaction diagram
-
-
-
?
2-dehydro-3-deoxy-D-glucarate
pyruvate + tartronate semialdehyde
show the reaction diagram
5-dehydro-4-deoxy-D-glucarate
pyruvate + tartronate semialdehyde
show the reaction diagram
Pyruvate + D-glyceraldehyde
?
show the reaction diagram
-
-
-
-
?
pyruvate + glyceraldehyde
?
show the reaction diagram
-
-
-
?
pyruvate + glycolaldehyde
2-oxo-4,5-dihydroxy-L-pentanoic acid
show the reaction diagram
Pyruvate + glyoxylate
?
show the reaction diagram
-
-
-
-
?
Pyruvate + L-glyceraldehyde
?
show the reaction diagram
-
-
-
-
?
pyruvate + tartronate semialdehyde
2-dehydro-3-deoxy-D-glucarate
show the reaction diagram
-
-
-
?
pyruvate + tartronate semialdehyde
5-dehydro-4-deoxy-D-glucarate
show the reaction diagram
-
-
-
?
additional information
?
-
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
additional information
?
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Co2+
requirement for divalent metal ion such as Mn2+, Mg2+ or Co2+
Mn2+
requirement for divalent metal ion such as Mn2+, Mg2+ or Co2+
Co2+
-
absolute cation requirement, activation in the order of increasing effectiveness: Mg2+, Co2+, Fe2+, Mn2+, Mo2+
Fe2+
-
absolute cation requirement, activation in the order of increasing effectiveness: Mg2+, Co2+, Fe2+, Mn2+, Mo2+
Mg2+
-
absolute cation requirement, activation in the order of increasing effectiveness: Mg2+, Co2+, Fe2+, Mn2+, Mo2+
Mn2+
-
absolute cation requirement, activation in the order of increasing effectiveness: Mg2+, Co2+, Fe2+, Mn2+, Mo2+
Mo2+
-
absolute cation requirement, activation in the order of increasing effectiveness: Mg2+, Co2+, Fe2+, Mn2+, Mo2+
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
CN-
-
reversed by Mg2+ and Co2+, but not by Fe2+
diphosphate
-
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.078
2-dehydro-3-deoxy-L-rhamnonic acid
data for Mg2+-activated YfaU
0.8
2-keto-3-deoxy-L-lyxonate
data for Mg2+-activated YfaU
0.14
2-keto-3-deoxy-L-mannonate
data for Mg2+-activated YfaU
0.1 - 0.15
4-hydroxy-2-ketoheptane-1,7-dioate
0.05
4-hydroxy-2-ketohexanoic acid
data for Ni2+-activated YfaU
0.1
4-hydroxy-2-ketopentanoic acid
data for Ni2+-activated YfaU
0.000065
5-dehydro-4-deoxy-D-glucarate
-
-
additional information
additional information
-
-
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.4
2-dehydro-3-deoxy-L-rhamnonic acid
data for Mg2+-activated YfaU
0.3
2-keto-3-deoxy-L-lyxonate
data for Mg2+-activated YfaU
0.3
2-keto-3-deoxy-L-mannonate
data for Mg2+-activated YfaU
0.54 - 299
4-hydroxy-2-ketoheptane-1,7-dioate
447
4-hydroxy-2-ketohexanoic acid
data for Ni2+-activated YfaU
396
4-hydroxy-2-ketopentanoic acid
data for Ni2+-activated YfaU
27.3
5-dehydro-4-deoxy-D-glucarate
-
-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
-
-
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
8
activity assay
7.7 - 8.6
-
-
8
-
assay at
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
overexpression of YagE increases cell viability in the presence of certain bactericidal antibiotics, indicating a putative biological role of YagE as a prophage encoded virulence factor enabling the survival of bacteria in the presence of certain antibiotics
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hexamer
crystallographic data
tetramer
x-ray crystallography
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
complexed with pyruvate
the crystal structure of apo-YfaU is determined to 1.39 A resolution and the structure of a Mg2+-pyruvate product complex to 1.93 A resolution
hanging drop vapor diffusion method
-
micro batch method, cocrystallization of YagE with 2-keto-3-deoxy galactonate and with pyruvate and glyceraldehyde in 100 mM HEPES pH 6.5, 200 mM MgCl2, 15% (w/v) PEG 3350, 50 mM pyruvate, and 50 mM glyceraldehyde
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6 - 7.5
-
stable
5078
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
using metal affinity and size exclusion chromatography
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
into the plasmid pT7 for expression in Escherichia coli B834DE3 pLacIRARE2 cells
expressed in Escherichia coli BL21 (DE3) cells
expression in Escherichia coli BL21
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
analysis
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Wood, W.A.
2-Keto-3-deoxy-6-phosphogluconic and related aldolases
The Enzymes, 3rd Ed. (Boyer, P. D. , ed. )
7
281-302
1972
Escherichia coli, no activity in Bacillus subtilis
-
Manually annotated by BRENDA team
Fish, D.C.; Blumenthal, H.J.
2-keto-3-deoxy-D-Glucarate aldolase
Methods Enzymol.
9
529-534
1966
Escherichia coli, Escherichia coli CR63MA
-
Manually annotated by BRENDA team
Marsh, C.A.
An enzymatic determination of D-glucaric acid by conversion to pyruvate
Anal. Biochem.
145
266-272
1985
Escherichia coli, Escherichia coli NCTC 10418
Manually annotated by BRENDA team
Blumenthal, H.J.; Lucuta, V.L.; Blumenthal, D.C.
Specific enzymatic assay for D-glucarate in human serum
Anal. Biochem.
185
286-293
1990
Escherichia coli
Manually annotated by BRENDA team
Hubbard, B.K.; Koch, M.; Palmer, D.R.J.; Babbitt, P.C.; Gerlt, J.A.
Evolution of enzymatic activities in the enolase superfamily: characterization of the (D)-glucarate/galactarate catabolic pathway in Escherichia coli
Biochemistry
37
14369-14375
1998
Escherichia coli
Manually annotated by BRENDA team
Blackwell, N.C.; Cullis, P.M.; Cooper, R.A.; Izard, T.
Rhombohedral crystals of 2-dehydro-3-deoxygalactarate aldolase from Escherichia coli
Acta Crystallogr. Sect. D
55
1368-1369
1999
Escherichia coli
-
Manually annotated by BRENDA team
Izard, T.; Blackwell, N.C.
Crystal structures of the metal-dependent 2-dehydro-3-deoxy-galactarate aldolase suggest a novel reaction mechanism
EMBO J.
19
3849-3856
2000
Escherichia coli (P23522), Escherichia coli
Manually annotated by BRENDA team
Rea, D.; Hovington, R.; Rakus, J.F.; Gerlt, J.A.; Fueloep, V.; Bugg, T.D.; Roper, D.I.
Crystal structure and functional assignment of YfaU, a metal ion dependent class II aldolase from Escherichia coli K12
Biochemistry
47
9955-9965
2008
Escherichia coli (P23522)
Manually annotated by BRENDA team
Bhaskar, V.; Kumar, M.; Manicka, S.; Tripathi, S.; Venkatraman, A.; Krishnaswamy, S.
Identification of biochemical and putative biological role of a xenolog from Escherichia coli using structural analysis
Proteins
79
1132-1142
2011
Escherichia coli (P75682), Escherichia coli
Manually annotated by BRENDA team