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Information on EC 4.1.3.17 - 4-hydroxy-4-methyl-2-oxoglutarate aldolase
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4.1.3.17 4-hydroxy-4-methyl-2-oxoglutarate aldolaseIUBMB Comments
Requires a divalent metal ion . This enzyme participates in the degradation of 3,4-dihydroxybenzoate (via the meta-cleavage pathway), phthalate, syringate and 3,4,5-trihydroxybenzoate [1-3]. The enzyme from Pseudomonas straminea can also catalyse the activity of EC 4.1.3.16, 4-hydroxy-2-oxoglutarate aldolase, and the decarboxylation of oxaloacetate .
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Word Map
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Reaction Schemes
Synonyms
4-hydroxy-4-methyl-2-oxoglutarate aldolase, hmg/cha aldolase, pyruvate aldolase, hmg aldolase, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
4-hydroxy-4-methyl-2-ketoglutarate aldolase
-
-
-
-
4-hydroxy-4-methyl-2-oxoglutarate aldolase
4-hydroxy-4-methyl-2-oxoglutarate/4-carboxy-4-hydroxy-2-oxoadipate aldolase
aldolase, 4-hydroxy-4-methyl-2-oxoglutarate
-
-
-
-
gamma-methyl-gamma-hydroxy-alpha-ketoglutaric aldolase
-
-
-
-
HMG aldolase
HMG/CHA aldolase
MHK aldolase
-
-
-
-
MHKG aldolase
-
-
-
-
pyruvate aldolase
-
-
-
-
4-hydroxy-4-methyl-2-oxoglutarate/4-carboxy-4-hydroxy-2-oxoadipate aldolase
-
-
4-hydroxy-4-methyl-2-oxoglutarate/4-carboxy-4-hydroxy-2-oxoadipate aldolase
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
2-hydroxy-4-oxobutane-1,2,4-tricarboxylate = oxaloacetate + pyruvate
(2)
-
-
-
4-hydroxy-4-methyl-2-oxoglutarate = 2 pyruvate
(1)
-
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
elimination
-
-
of an oxo-acid, C-C bond cleavage
-
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PATHWAY SOURCE
PATHWAYS
BRENDA
KEGG
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SYSTEMATIC NAME
IUBMB Comments
4-hydroxy-4-methyl-2-oxoglutarate pyruvate-lyase (pyruvate-forming)
Requires a divalent metal ion [3]. This enzyme participates in the degradation of 3,4-dihydroxybenzoate (via the meta-cleavage pathway), phthalate, syringate and 3,4,5-trihydroxybenzoate [1-3]. The enzyme from Pseudomonas straminea can also catalyse the activity of EC 4.1.3.16, 4-hydroxy-2-oxoglutarate aldolase, and the decarboxylation of oxaloacetate [3].
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CAS REGISTRY NUMBER
COMMENTARY
37290-65-6
-
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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
4-hydroxy-4-methyl-2-oxoglutarate
pyruvate
-
involved in biosynthesis of gamma-substituted glutamic acid, participates in the alpha-keto acid pathway for degradation of the meta-fission product of protocatechuate, in Pseudomonas ochraceae grown on phthalate the physiolological substrate is not hydroxymethyl glutamic acid but CHA, L-4-carboxy-4-hydroxy-2-oxoadipate, which is cleaved to pyruvate and oxaloacetate
-
r
4-carboxy-4-hydroxy-2-oxoadipate
pyruvate + oxaloacetate
-
the L-isomer is preferred
-
?
4-carboxy-4-hydroxy-2-oxoadipate
pyruvate + oxaloacetate
-
no equilibrium due to oxaloacetate beta-decarboxylase activity associated with the enzyme
-
?
4-carboxy-4-hydroxy-2-oxoadipate
pyruvate + oxaloacetate
-
L-4-carboxy-4-hydroxy-2-oxoadipate or D-4-carboxy-4-hydroxy-2-oxoadipate
-
?
4-Hydroxy-2-oxoglutarate
Pyruvate + glyoxylate
-
the L-isomer is preferred
-
?
4-hydroxy-4-methyl-2-oxoglutarate
2 pyruvate
Thermus thermophilus HB8 / ATCC 27634 / DSM 579
-
-
-
-
?
4-hydroxy-4-methyl-2-oxoglutarate
pyruvate + pyruvate
-
preferentially attacks the R-form of 4-hydroxy-4-methyl-2-oxoglutarate
-
?
4-hydroxy-4-methyl-2-oxoglutarate
pyruvate + pyruvate
-
the enzyme attacks only one enantiomer
-
?
4-hydroxy-4-methyl-2-oxoglutarate
pyruvate + pyruvate
-
the L-isomer is preferred
-
?
D-4-carboxy-4-hydroxy-2-oxoadipate
pyruvate + oxaloacetate
-
-
-
?
D-4-carboxy-4-hydroxy-2-oxoadipate
pyruvate + oxaloacetate
-
-
-
?
DL-4-carboxy-4-hydroxy-2-oxoadipate
pyruvate + oxaloacetate
-
-
-
?
DL-4-carboxy-4-hydroxy-2-oxoadipate
pyruvate + oxaloacetate
-
-
-
?
l-4-carboxy-4-hydroxy-2-oxoadipate
pyruvate + oxaloacetate
-
-
-
?
l-4-carboxy-4-hydroxy-2-oxoadipate
pyruvate + oxaloacetate
-
-
-
?
additional information
?
-
-
the enzyme is a class II, divalent metal ion-dependent, pyruvate aldolase that catalyzes the aldol cleavage of 4-hydroxy-4-methyl-2-oxoglutarate and 4-carboxy-4-hydroxy-2-oxoadipate into two molecules of pyruvate in the former and a molecule of each pyruvate and oxaloacetate in the latter, cf. 4-carboxy-4-hydroxy-2-oxoadipate aldolase, EC 4.1.3. The enzyme also contains a secondary oxaloacetate decarboxylase activity due to the common pyruvate enolate transition state formed following C-C bond cleavage in the retroaldol and decarboxylase reactions
-
-
?
additional information
?
-
-
inducible by aromatic carboxylates such as phthalate
-
-
?
additional information
?
-
-
the RNAse E activity A-like protein Yer010Cp from Saccharomyces cerevisiae S288C contains HMG aldolase and oxaloacetate decarboxylase activities
-
-
?
additional information
?
-
-
the RNAse E activity A-like protein TtRraA from Thermus thermophilus HB8 contains HMG aldolase and oxaloacetate decarboxylase activities
-
-
?
additional information
?
-
Thermus thermophilus HB8 / ATCC 27634 / DSM 579
-
the RNAse E activity A-like protein TtRraA from Thermus thermophilus HB8 contains HMG aldolase and oxaloacetate decarboxylase activities
-
-
?
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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
4-hydroxy-4-methyl-2-oxoglutarate
pyruvate
-
involved in biosynthesis of gamma-substituted glutamic acid, participates in the alpha-keto acid pathway for degradation of the meta-fission product of protocatechuate, in Pseudomonas ochraceae grown on phthalate the physiolological substrate is not hydroxymethyl glutamic acid but CHA, L-4-carboxy-4-hydroxy-2-oxoadipate, which is cleaved to pyruvate and oxaloacetate
-
r
l-4-carboxy-4-hydroxy-2-oxoadipate
pyruvate + oxaloacetate
-
-
-
?
l-4-carboxy-4-hydroxy-2-oxoadipate
pyruvate + oxaloacetate
-
-
-
?
additional information
?
-
-
the enzyme is a class II, divalent metal ion-dependent, pyruvate aldolase that catalyzes the aldol cleavage of 4-hydroxy-4-methyl-2-oxoglutarate and 4-carboxy-4-hydroxy-2-oxoadipate into two molecules of pyruvate in the former and a molecule of each pyruvate and oxaloacetate in the latter, cf. 4-carboxy-4-hydroxy-2-oxoadipate aldolase, EC 4.1.3. The enzyme also contains a secondary oxaloacetate decarboxylase activity due to the common pyruvate enolate transition state formed following C-C bond cleavage in the retroaldol and decarboxylase reactions
-
-
?
additional information
?
-
-
inducible by aromatic carboxylates such as phthalate
-
-
?
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Cd2+
Co2+
Mg2+
Mn2+
Ni2+
Zn2+
-
absolute requirement for divalent metal ion: Mg2+, Mn2+, Co2+, Zn2+ or Cd2+, Km: 0.0018 mM, reaction with L-4-carboxy-4-hydroxy-2-oxoadipate
additional information
Cd2+
-
absolute requirement for divalent metal ion: Mg2+, Mn2+, Co2+, Zn2+ or Cd2+
Co2+
-
required, best activating metal ion, Km is 0.00838 mM for the wild-type enzyme, and 0.446 mM for the mutant E199A
Co2+
-
absolute requirement for divalent metal ion: Mg2+, Mn2+, Co2+, Zn2+ or Cd2+
Mg2+
-
a magnesium ion is coordinated directly or indirectly via water through interactions with Asp102, Asp124, and Glu199
Mg2+
-
absolute requirement for divalent metal ion: Mg2+, Mn2+, Co2+, Zn2+ or Cd2+
Mn2+
-
absolute requirement for divalent metal ion: Mg2+, Mn2+, Co2+, Zn2+ or Cd2+
additional information
-
the enzyme is a class II divalent metal ion-dependent aldolase. Coordination of a metal ion to support the binding of a pyruvyl moiety in the class II aldolase is essential, metal binding Glu199 residue
additional information
-
the enzyme is a class II divalent metal ion-dependent aldolase
additional information
-
the enzyme is a class II divalent metal ion-dependent aldolase
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
2-oxoadipate
-
competitive with respect to DL-4-carboxy-4-hydroxy-2-oxoadipate
2-oxobutanoate
-
competitive with respect to DL-4-carboxy-4-hydroxy-2-oxoadipate
4-hydroxy-2-oxobutyrate
-
competitive with respect to DL-4-carboxy-4-hydroxy-2-oxoadipate
diethyl dicarbonate
-
not reversed by hydroxylamine, L-4-carboxy-4-hydroxy-2-oxoadipate strongly protects against inactivation
DL-4-hydroxy-2-oxovalerate
-
competitive with respect to DL-4-carboxy-4-hydroxy-2-oxoadipate
2-oxoglutarate
-
competitive with respect to DL-4-carboxy-4-hydroxy-2-oxoadipate
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
neither 2 mM Na2SO4 nor Na2MoO4 activate the enzyme
-
phosphate
the enzyme is uncompetitively activated in the presence of phosphate
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.071
2-hydroxy-4-oxopentanedioic acid
-
wild type protein, 1.0 mM Mn2+, pH 8.0, 25°C
0.15
2-hydroxy-4-oxopentanedioic acid
-
wild type protein, 1.0 mM Mg2+, pH 8.0, 25°C
0.015
4-carboxy-4-hydroxy-2-oxoadipate
wild type enzyme, in the absence of phosphate, at pH 8.0 and 25°C
0.104
4-carboxy-4-hydroxy-2-oxoadipate
wild type enzyme, in the presence of 2 mM phosphate, at pH 8.0 and 25°C
8.8
4-hydroxy-2-oxopentanoate
-
wild type protein, 1.0 mM Mn2+, pH 8.0, 25°C
25
4-hydroxy-2-oxopentanoate
-
wild type protein, 1.0 mM Mg2+, pH 8.0, 25°C
0.022
4-hydroxy-4-methyl-2-oxoglutarate
-
wild type protein, 1.0 mM Mn2+, pH 8.0, 25°C
0.1265
4-hydroxy-4-methyl-2-oxoglutarate
-
pH 8.0, 25°C, RraA-like protein Yer010Cp
0.1507
4-hydroxy-4-methyl-2-oxoglutarate
-
pH 8.0, 25°C, RraA-like protein TtRraA
0.188
4-hydroxy-4-methyl-2-oxoglutarate
wild type enzyme, in the absence of phosphate, at pH 8.0 and 25°C
0.26
4-hydroxy-4-methyl-2-oxoglutarate
-
wild type protein, 1.0 mM Mg2+, pH 8.0, 25°C
0.304
4-hydroxy-4-methyl-2-oxoglutarate
mutant enzyme R40A, in the absence of phosphate, at pH 8.0 and 25°C
0.389
4-hydroxy-4-methyl-2-oxoglutarate
mutant enzyme H75A, in the absence of phosphate, at pH 8.0 and 25°C
0.796
4-hydroxy-4-methyl-2-oxoglutarate
mutant enzyme N71A, in the absence of phosphate, at pH 8.0 and 25°C
1.08
4-hydroxy-4-methyl-2-oxoglutarate
mutant enzyme T145A, in the absence of phosphate, at pH 8.0 and 25°C
1.11
4-hydroxy-4-methyl-2-oxoglutarate
mutant enzyme N71A, in the presence of 2 mM phosphate, at pH 8.0 and 25°C
1.21
4-hydroxy-4-methyl-2-oxoglutarate
mutant enzyme H75A, in the presence of 2 mM phosphate, at pH 8.0 and 25°C
1.36
4-hydroxy-4-methyl-2-oxoglutarate
wild type enzyme, in the presence of 2 mM phosphate, at pH 8.0 and 25°C
1.37
4-hydroxy-4-methyl-2-oxoglutarate
mutant enzyme R195A, in the absence of phosphate, at pH 8.0 and 25°C
1.39
4-hydroxy-4-methyl-2-oxoglutarate
mutant enzyme G144V, in the absence of phosphate, at pH 8.0 and 25°C
1.78
4-hydroxy-4-methyl-2-oxoglutarate
mutant enzyme T145A, in the presence of 2 mM phosphate, at pH 8.0 and 25°C
2.01
4-hydroxy-4-methyl-2-oxoglutarate
mutant enzyme K147A, in the absence of phosphate, at pH 8.0 and 25°C
2.89
4-hydroxy-4-methyl-2-oxoglutarate
mutant enzyme R195A, in the presence of 2 mM phosphate, at pH 8.0 and 25°C
3.21
4-hydroxy-4-methyl-2-oxoglutarate
mutant enzyme R123K, in the absence of phosphate, at pH 8.0 and 25°C
3.26
4-hydroxy-4-methyl-2-oxoglutarate
mutant enzyme R40A, in the presence of 2 mM phosphate, at pH 8.0 and 25°C
3.72
4-hydroxy-4-methyl-2-oxoglutarate
mutant enzyme K147A, in the presence of 2 mM phosphate, at pH 8.0 and 25°C
3.97
4-hydroxy-4-methyl-2-oxoglutarate
mutant enzyme R123K, in the presence of 2 mM phosphate, at pH 8.0 and 25°C
5.5
4-hydroxy-4-methyl-2-oxoglutarate
-
R123K mutant protein, pH 8.0, 25°C
6.83
4-hydroxy-4-methyl-2-oxoglutarate
mutant enzyme G144V, in the presence of 2 mM phosphate, at pH 8.0 and 25°C
0.036
oxaloacetate
-
wild type protein, 1.0 mM Mn2+, pH 8.0, 25°C; substrate inhibition constante 0.25 mM
0.298
oxaloacetate
wild type enzyme, in the absence of phosphate, at pH 8.0 and 25°C
0.3
oxaloacetate
-
wild type protein, 1.0 mM Mg2+, pH 8.0, 25°C; substrate inhibition constante 0.37 mM
0.741
oxaloacetate
wild type enzyme, in the presence of 2 mM phosphate, at pH 8.0 and 25°C
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.058
2-hydroxy-4-oxopentanedioic acid
-
wild type protein, 1.0 mM Mg2+, pH 8.0, 25°C
0.25
2-hydroxy-4-oxopentanedioic acid
-
wild type protein, 1.0 mM Mn2+, pH 8.0, 25°C
13.4
4-carboxy-4-hydroxy-2-oxoadipate
wild type enzyme, in the absence of phosphate, at pH 8.0 and 25°C
145
4-carboxy-4-hydroxy-2-oxoadipate
wild type enzyme, in the presence of 2 mM phosphate, at pH 8.0 and 25°C
0.048
4-hydroxy-2-oxopentanoate
-
wild type protein, 1.0 mM Mg2+, pH 8.0, 25°C
0.19
4-hydroxy-2-oxopentanoate
-
wild type protein, 1.0 mM Mn2+, pH 8.0, 25°C
0.014
4-hydroxy-4-methyl-2-oxoglutarate
mutant enzyme K147A, in the absence of phosphate, at pH 8.0 and 25°C
0.014
4-hydroxy-4-methyl-2-oxoglutarate
mutant enzyme N71A, in the absence of phosphate, at pH 8.0 and 25°C
0.0184
4-hydroxy-4-methyl-2-oxoglutarate
mutant enzyme N71A, in the presence of 2 mM phosphate, at pH 8.0 and 25°C
0.0224
4-hydroxy-4-methyl-2-oxoglutarate
mutant enzyme K147A, in the presence of 2 mM phosphate, at pH 8.0 and 25°C
0.0276
4-hydroxy-4-methyl-2-oxoglutarate
-
pH 8.0, 25°C, RraA-like protein Yer010Cp
0.07
4-hydroxy-4-methyl-2-oxoglutarate
mutant enzyme R123K, in the presence of 2 mM phosphate, at pH 8.0 and 25°C
0.086
4-hydroxy-4-methyl-2-oxoglutarate
mutant enzyme R123K, in the absence of phosphate, at pH 8.0 and 25°C
0.099
4-hydroxy-4-methyl-2-oxoglutarate
-
R123K mutant protein, pH 8.0, 25°C
0.215
4-hydroxy-4-methyl-2-oxoglutarate
mutant enzyme G144V, in the absence of phosphate, at pH 8.0 and 25°C
0.356
4-hydroxy-4-methyl-2-oxoglutarate
-
pH 8.0, 25°C, RraA-like protein TtRraA
0.394
4-hydroxy-4-methyl-2-oxoglutarate
mutant enzyme G144V, in the presence of 2 mM phosphate, at pH 8.0 and 25°C
0.889
4-hydroxy-4-methyl-2-oxoglutarate
mutant enzyme T145A, in the absence of phosphate, at pH 8.0 and 25°C
6.7
4-hydroxy-4-methyl-2-oxoglutarate
mutant enzyme R40A, in the absence of phosphate, at pH 8.0 and 25°C
6.72
4-hydroxy-4-methyl-2-oxoglutarate
mutant enzyme R195A, in the absence of phosphate, at pH 8.0 and 25°C
10.7
4-hydroxy-4-methyl-2-oxoglutarate
mutant enzyme T145A, in the presence of 2 mM phosphate, at pH 8.0 and 25°C
11.5
4-hydroxy-4-methyl-2-oxoglutarate
mutant enzyme R195A, in the presence of 2 mM phosphate, at pH 8.0 and 25°C
13.7
4-hydroxy-4-methyl-2-oxoglutarate
-
wild type protein, 1.0 mM Mn2+, pH 8.0, 25°C
15.6
4-hydroxy-4-methyl-2-oxoglutarate
wild type enzyme, in the absence of phosphate, at pH 8.0 and 25°C
19.3
4-hydroxy-4-methyl-2-oxoglutarate
-
wild type protein, 1.0 mM Mg2+, pH 8.0, 25°C
22.3
4-hydroxy-4-methyl-2-oxoglutarate
mutant enzyme H75A, in the absence of phosphate, at pH 8.0 and 25°C
36.6
4-hydroxy-4-methyl-2-oxoglutarate
mutant enzyme R40A, in the presence of 2 mM phosphate, at pH 8.0 and 25°C
53.5
4-hydroxy-4-methyl-2-oxoglutarate
mutant enzyme H75A, in the presence of 2 mM phosphate, at pH 8.0 and 25°C
134
4-hydroxy-4-methyl-2-oxoglutarate
wild type enzyme, in the presence of 2 mM phosphate, at pH 8.0 and 25°C
1.86
oxaloacetate
wild type enzyme, in the absence of phosphate, at pH 8.0 and 25°C
3.16
oxaloacetate
wild type enzyme, in the presence of 2 mM phosphate, at pH 8.0 and 25°C
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.38
2-hydroxy-4-oxopentanedioic acid
-
wild type protein, 1.0 mM Mg2+, pH 8.0, 25°C
3.5
2-hydroxy-4-oxopentanedioic acid
-
wild type protein, 1.0 mM Mn2+, pH 8.0, 25°C
893
4-carboxy-4-hydroxy-2-oxoadipate
wild type enzyme, in the absence of phosphate, at pH 8.0 and 25°C
1400
4-carboxy-4-hydroxy-2-oxoadipate
wild type enzyme, in the presence of 2 mM phosphate, at pH 8.0 and 25°C
0.0019
4-hydroxy-2-oxopentanoate
-
wild type protein, 1.0 mM Mg2+, pH 8.0, 25°C
0.022
4-hydroxy-2-oxopentanoate
-
wild type protein, 1.0 mM Mn2+, pH 8.0, 25°C
0.00645
4-hydroxy-4-methyl-2-oxoglutarate
mutant enzyme K147A, in the presence of 2 mM phosphate, at pH 8.0 and 25°C
0.00697
4-hydroxy-4-methyl-2-oxoglutarate
mutant enzyme K147A, in the absence of phosphate, at pH 8.0 and 25°C
0.0165
4-hydroxy-4-methyl-2-oxoglutarate
mutant enzyme N71A, in the presence of 2 mM phosphate, at pH 8.0 and 25°C
0.0176
4-hydroxy-4-methyl-2-oxoglutarate
mutant enzyme N71A, in the absence of phosphate, at pH 8.0 and 25°C
0.0176
4-hydroxy-4-methyl-2-oxoglutarate
mutant enzyme R123K, in the presence of 2 mM phosphate, at pH 8.0 and 25°C
0.0267
4-hydroxy-4-methyl-2-oxoglutarate
mutant enzyme R123K, in the absence of phosphate, at pH 8.0 and 25°C
0.0577
4-hydroxy-4-methyl-2-oxoglutarate
mutant enzyme G144V, in the presence of 2 mM phosphate, at pH 8.0 and 25°C
0.155
4-hydroxy-4-methyl-2-oxoglutarate
mutant enzyme G144V, in the absence of phosphate, at pH 8.0 and 25°C
0.823
4-hydroxy-4-methyl-2-oxoglutarate
mutant enzyme T145A, in the absence of phosphate, at pH 8.0 and 25°C
3.98
4-hydroxy-4-methyl-2-oxoglutarate
mutant enzyme R195A, in the presence of 2 mM phosphate, at pH 8.0 and 25°C
4.91
4-hydroxy-4-methyl-2-oxoglutarate
mutant enzyme R195A, in the absence of phosphate, at pH 8.0 and 25°C
6.01
4-hydroxy-4-methyl-2-oxoglutarate
mutant enzyme T145A, in the presence of 2 mM phosphate, at pH 8.0 and 25°C
11.2
4-hydroxy-4-methyl-2-oxoglutarate
mutant enzyme R40A, in the presence of 2 mM phosphate, at pH 8.0 and 25°C
22
4-hydroxy-4-methyl-2-oxoglutarate
mutant enzyme R40A, in the absence of phosphate, at pH 8.0 and 25°C
44.5
4-hydroxy-4-methyl-2-oxoglutarate
mutant enzyme H75A, in the presence of 2 mM phosphate, at pH 8.0 and 25°C
57.3
4-hydroxy-4-methyl-2-oxoglutarate
mutant enzyme H75A, in the absence of phosphate, at pH 8.0 and 25°C
74
4-hydroxy-4-methyl-2-oxoglutarate
-
wild type protein, 1.0 mM Mg2+, pH 8.0, 25°C
83
4-hydroxy-4-methyl-2-oxoglutarate
wild type enzyme, in the absence of phosphate, at pH 8.0 and 25°C
98.5
4-hydroxy-4-methyl-2-oxoglutarate
wild type enzyme, in the presence of 2 mM phosphate, at pH 8.0 and 25°C
210
4-hydroxy-4-methyl-2-oxoglutarate
-
pH 8.0, 25°C, RraA-like protein Yer010Cp
620
4-hydroxy-4-methyl-2-oxoglutarate
-
wild type protein, 1.0 mM Mn2+, pH 8.0, 25°C
2400
4-hydroxy-4-methyl-2-oxoglutarate
-
pH 8.0, 25°C, RraA-like protein TtRraA
4.26
oxaloacetate
wild type enzyme, in the presence of 2 mM phosphate, at pH 8.0 and 25°C
6.24
oxaloacetate
wild type enzyme, in the absence of phosphate, at pH 8.0 and 25°C
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7.7
-
L-4-carboxy-4-hydroxy-2-oxoadipate, in presence of 0.2 mM phosphate
8.3
8.4
-
DL-4-hydroxy-4-methyl-2-oxoglutarate, in presence of 0.2 mM phosphate
8.9
8.3
-
L-4-carboxy-4-hydroxy-2-oxoadipate, in presence of 0.2 mM phosphate
8.9
-
DL-4-hydroxy-4-methyl-2-oxoglutarate or oxaloacetate, with 3 mM phosphate
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7.5 - 9.5
-
pH 7.5: about 30% of maximal activity, pH 9.5: about 65% of maximal activity
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
25
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pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
development of a selection strategy for the evolution of the substrate specificity of KDPG aldolase based on a pyruvate kinase-deficient strain of Escherichia coli
-
-
brenda
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
metabolism
-
4-hydroxy-4-methyl-2-oxoglutarate/4-carboxy-4-hydroxy-2-oxoadipate aldolases are class II pyruvate aldolases from the meta cleavage pathways of protocatechuate and gallate
additional information
-
the Pseudomonas putida F1 HMG/CHA aldolase has a D-X20-R-D motif, active site structure, structure-function relationship, overview. The Glu199 residue in HMG/CHA aldolase positions one water molecule and in concert with the Asp102 residue positions a second water molecule that coordinate with the bound magnesium ion
evolution
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RNase E activity A, RraA, like protein (RraA-like protein) TtRraA from Thermus thermophilus HB8 (TtRraA) contains HMG aldolase and oxaloacetate decarboxylase activities. The enzyme TtRraA contains a G-X20-R-D-X2-E/D motif
evolution
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RNase E activity A, RraA, like proteins TtRraA and Yer010Cp from Thermus thermophilus HB8 (TtRraA) and Saccharomyces cerevisiae S288C (Yer010Cp) contain HMG aldolase and oxaloacetate decarboxylase activities and a G-X20-R-D-X2-E/D motif, that may support metal binding. The Pseudomonas putida F1 HMG/CHA aldolase has a D-X20-R-D motif. Structural and fucntional relationships of the HMG/CHA aldolase and RraA-like proteins, overview
evolution
-
RNase E activity A-like protein (RraA-like protein) Yer010Cp from Saccharomyces cerevisiae S288C contains HMG aldolase and oxaloacetate decarboxylase activities. The enzyme Yer010Cp contains a G-X20-R-D-X2-E/D motif
evolution
Thermus thermophilus HB8 / ATCC 27634 / DSM 579
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RNase E activity A, RraA, like protein (RraA-like protein) TtRraA from Thermus thermophilus HB8 (TtRraA) contains HMG aldolase and oxaloacetate decarboxylase activities. The enzyme TtRraA contains a G-X20-R-D-X2-E/D motif
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Show AA Sequence and Transmembrane Helices (10314 entries)
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PDB
SCOP
CATH
UNIPROT
ORGANISM
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
24070
-
calculated from amino acid sequence corresponding to gene sequence
26000
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hexamer
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
E199A
-
site-directed mutagenesis, the mutant shows reduced activity and reduced affinity for Co2+ compared to the wild-type enzyme
G144V
the variant has a 10fold increase in KM and a 73fold decrease in kcat for the 4-hydroxy-4-methyl-2-oxoglutarate cleavage reaction and the kcat increases 2-fold in the presence of phosphate
H75A
the variant has a 2fold increase in KM and a 1.4fold increase in kcat for the 4-hydroxy-4-methyl-2-oxoglutarate catalyzed reaction and does not have a significant effect on the pyruvate methyl proton exchange rate compared to the wild type enzyme
K147A
the mutation has significant effects on the steady state kinetics of the aldolase 4-hydroxy-4-methyl-2-oxoglutarate reaction with decreasing the kcat by 1114fold compared to the wild type enzyme
N71A
the mutation has significant effects on the steady state kinetics of the aldolase 4-hydroxy-4-methyl-2-oxoglutarate reaction with decreasing the kcat by 1114fold compared to the wild type enzyme
R123K
R195A
the substitution moderately effects the 4-hydroxy-4-methyl-2-oxoglutarate cleavage reaction with a 7fold increase in KM and a 2fold decrease in kcat. The activation of kcat and the pyruvate methyl proton exchange rate by Pi is each reduced by 5fold
R40A
the variant has a 2fold decrease in kcat and is still activated to a similar extent as the wild type enzyme in the 4-hydroxy-4-methyl-2-oxoglutarate aldolase cleavage reaction
T145A
the variant is activated in the presence of phosphate resulting in a 12fold increase in kcat for the 4-hydroxy-4-methyl-2-oxoglutarate catalyzed reaction and a 24fold increase in the pyruvate methyl proton exchange rate compared to the wild type enzyme
R123K
the mutation reduces the kcat of the 4-hydroxy-4-methyl-2-oxoglutarate catalyzed reaction by 181fold and reduces the pyruvate methyl proton exchange rate by 20fold compared to the wild type enzyme
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pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
ion exchange chromatography, hydrophobic interaction chromatography, gel filtration
-
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
DNA fragment carrying the gene proA from chromosomal DNA cloned and overproduced in Escherichia coli XL1-Blue MRF'
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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
Arachis hypogaea
-
brenda
Shannon, L.M.; Marcus, A.
gamma-Methyl-gamma-hydroxy-alpha-ketoglutaric aldolase
J. Biol. Chem.
237
3342-3347
1962
Arachis hypogaea
brenda
Tack, B.F.; Chapman, P.J.; Dagley, S.
Purification and properties of 4-hydroxy-4-methyl-2-oxoglutarate aldolase
J. Biol. Chem.
247
6444-6449
1972
Pseudomonas putida
brenda
Schuld Ritter, C.; Chapman, P.J.; Dagley, S.
Absolute configuration of a metabolite in the m-fission pathway of protocatechuate
J. Bacteriol.
113
1064-1065
1973
Comamonas testosteroni
brenda
Dagley, S.
4-Hydroxy-4-methyl-2-ketoglutarate aldolase from Pseudomonas putida
Methods Enzymol.
90
272-276
1982
Pseudomonas putida
brenda
Maruyama, K.
Activation of Pseudomonas ochraceae 4-hydroxy-4-methyl-2-oxoglutarate aldolase by inorganic phosphate
J. Biochem.
10
334-340
1990
Pseudomonas straminea
brenda
Maruyama, K.
Purification and properties of 4-hydroxy-4-methyl-2-oxoglutarate aldolase from Pseudomonas ochraceae grown on phthalate
J. Biochem.
108
327-333
1990
Pseudomonas straminea
brenda
Maruyama, K.
Chemical modification of Pseudomonas ochraceae 4-hydroxy-4-methyl-2-oxoglutarate aldolase by diethyl pyrocarbonate
J. Biochem.
110
976-981
1991
Pseudomonas straminea
brenda
Maruyama, K.; Miwa, M.; Tsujii, N.; Nagai, T.; Tomita, N.; Harada, T.; Sobajima, H.; Sugisaki, H.
Cloning, sequencing, and expression of the gene encoding 4-hydroxy-4-methyl-2-oxoglutarate aldolase from Pseudomonas ochraceae NGJ1
Biosci. Biotechnol. Biochem.
65
2701-2709
2001
Pseudomonas straminea, Pseudomonas straminea NGJ1
brenda
Griffiths, J.S.; Cheriyan, M.; Corbell, J.B.; Pocivavsek, L.; Fierke, C.A.; Toone, E.J.
A bacterial selection for the directed evolution of pyruvate aldolases
Bioorg. Med. Chem.
12
4067-4074
2004
Escherichia coli
brenda
Wang, W.; Mazurkewich, S.; Kimber, M.S.; Seah, S.Y.
Structural and kinetic characterization of 4-hydroxy-4-methyl-2-oxoglutarate/4-carboxy-4-hydroxy-2-oxoadipate aldolase, a protocatechuate degradation enzyme evolutionarily convergent with the HpaI and DmpG pyruvate aldolases
J. Biol. Chem.
285
36608-36615
2010
Pseudomonas putida
brenda
Mazurkewich, S.; Wang, W.; Seah, S.Y.
Biochemical and structural analysis of RraA proteins to decipher their relationships with 4-hydroxy-4-methyl-2-oxoglutarate/4-carboxy-4-hydroxy-2-oxoadipate aldolases
Biochemistry
53
542-553
2014
Saccharomyces cerevisiae, Thermus thermophilus, Pseudomonas putida, Thermus thermophilus HB8 / ATCC 27634 / DSM 579
brenda
Mazurkewich, S.; Seah, S.Y.
Investigation into the mode of phosphate activation in the 4-hydroxy-4-methyl-2-oxoglutarate/4-carboxy-4-hydroxy-2-oxoadipate aldolase from Pseudomonas putida F1
PLoS ONE
11
e0164556
2016
Pseudomonas putida (A5W059)
brenda
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