BRENDA - Enzyme Database
show all sequences of 4.1.2.52

Structure and mechanism of HpcH: a metal ion dependent class II aldolase from the homoprotocatechuate degradation pathway of Escherichia coli

Rea, D.; Fulop, V.; Bugg, T.D.; Roper, D.I.; J. Mol. Biol. 373, 866-876 (2007)

Data extracted from this reference:

Cloned(Commentary)
Cloned (Commentary)
Organism
HpcH gene expressed in Escherichia coli strain B834 (DE3)
Escherichia coli
Crystallization (Commentary)
Crystallization (Commentary)
Organism
crystallization of apo-HpcH, because divalent metal ion is lost during the purification process, resulting in preparation of the inactive apo form of the enzyme, crystals grown using the hanging-drop vapour diffusion method; HpcH–Mg2+–oxamate crystals grown with the addition of 10 mM magnesium chloride and sodium oxamate (substrate analogue), elucidation of active site architecture
Escherichia coli
Molecular Weight [Da]
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
28000
-
-
Escherichia coli
Natural Substrates/ Products (Substrates)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
ID
4-hydroxy-2-oxo-heptanedioate
Escherichia coli
-
pyruvate + succinic semialdehyde
-
-
?
Organism
Organism
UniProt
Commentary
Textmining
Escherichia coli
-
-
-
Purification (Commentary)
Purification (Commentary)
Organism
metal affinity and size exclusion chromatography, Superdex 200 column used
Escherichia coli
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
Substrate Product ID
4-hydroxy-2-oxo-heptanedioate
-
722955
Escherichia coli
pyruvate + succinic semialdehyde
-
-
-
?
Subunits
Subunits
Commentary
Organism
hexamer
6 * 28000
Escherichia coli
Synonyms
Synonyms
Commentary
Organism
4-hydroxy-2-oxo-heptane-1,7-dioate aldolase
-
Escherichia coli
HpcH
-
Escherichia coli
Cloned(Commentary) (protein specific)
Commentary
Organism
HpcH gene expressed in Escherichia coli strain B834 (DE3)
Escherichia coli
Crystallization (Commentary) (protein specific)
Crystallization
Organism
crystallization of apo-HpcH, because divalent metal ion is lost during the purification process, resulting in preparation of the inactive apo form of the enzyme, crystals grown using the hanging-drop vapour diffusion method; HpcH–Mg2+–oxamate crystals grown with the addition of 10 mM magnesium chloride and sodium oxamate (substrate analogue), elucidation of active site architecture
Escherichia coli
Molecular Weight [Da] (protein specific)
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
28000
-
-
Escherichia coli
Natural Substrates/ Products (Substrates) (protein specific)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
ID
4-hydroxy-2-oxo-heptanedioate
Escherichia coli
-
pyruvate + succinic semialdehyde
-
-
?
Purification (Commentary) (protein specific)
Commentary
Organism
metal affinity and size exclusion chromatography, Superdex 200 column used
Escherichia coli
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
ID
4-hydroxy-2-oxo-heptanedioate
-
722955
Escherichia coli
pyruvate + succinic semialdehyde
-
-
-
?
Subunits (protein specific)
Subunits
Commentary
Organism
hexamer
6 * 28000
Escherichia coli
General Information
General Information
Commentary
Organism
metabolism
enzyme is part of homoprotocatechuate degradation pathway
Escherichia coli
General Information (protein specific)
General Information
Commentary
Organism
metabolism
enzyme is part of homoprotocatechuate degradation pathway
Escherichia coli
Other publictions for EC 4.1.2.52
No.
1st author
Pub Med
title
organims
journal
volume
pages
year
Activating Compound
Application
Cloned(Commentary)
Crystallization (Commentary)
Engineering
General Stability
Inhibitors
KM Value [mM]
Localization
Metals/Ions
Molecular Weight [Da]
Natural Substrates/ Products (Substrates)
Organic Solvent Stability
Organism
Oxidation Stability
Posttranslational Modification
Purification (Commentary)
Reaction
Renatured (Commentary)
Source Tissue
Specific Activity [micromol/min/mg]
Storage Stability
Substrates and Products (Substrate)
Subunits
Synonyms
Temperature Optimum [°C]
Temperature Range [°C]
Temperature Stability [°C]
Turnover Number [1/s]
pH Optimum
pH Range
pH Stability
Cofactor
Ki Value [mM]
pI Value
IC50 Value
Activating Compound (protein specific)
Application (protein specific)
Cloned(Commentary) (protein specific)
Cofactor (protein specific)
Crystallization (Commentary) (protein specific)
Engineering (protein specific)
General Stability (protein specific)
IC50 Value (protein specific)
Inhibitors (protein specific)
Ki Value [mM] (protein specific)
KM Value [mM] (protein specific)
Localization (protein specific)
Metals/Ions (protein specific)
Molecular Weight [Da] (protein specific)
Natural Substrates/ Products (Substrates) (protein specific)
Organic Solvent Stability (protein specific)
Oxidation Stability (protein specific)
Posttranslational Modification (protein specific)
Purification (Commentary) (protein specific)
Renatured (Commentary) (protein specific)
Source Tissue (protein specific)
Specific Activity [micromol/min/mg] (protein specific)
Storage Stability (protein specific)
Substrates and Products (Substrate) (protein specific)
Subunits (protein specific)
Temperature Optimum [°C] (protein specific)
Temperature Range [°C] (protein specific)
Temperature Stability [°C] (protein specific)
Turnover Number [1/s] (protein specific)
pH Optimum (protein specific)
pH Range (protein specific)
pH Stability (protein specific)
pI Value (protein specific)
Expression
General Information
General Information (protein specific)
Expression (protein specific)
KCat/KM [mM/s]
KCat/KM [mM/s] (protein specific)
725493
Coincon
Crystal structure of reaction ...
Escherichia coli
J. Biol. Chem.
287
36208-36221
2012
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-
-
1
5
-
-
4
-
1
-
1
-
1
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3
1
2
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4
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1
5
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4
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1
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1
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3
1
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4
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3
3
702377
Wang
Comparison of two metal-depend ...
Escherichia coli
Biochemistry
49
3774-3782
2010
-
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1
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-
5
10
-
1
-
1
-
1
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1
-
-
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9
-
1
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9
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6
-
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1
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5
6
10
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1
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1
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-
9
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-
-
-
9
-
-
-
-
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-
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9
9
722258
Wang
The role of a conserved histid ...
Escherichia coli
FEBS Lett.
582
3385-3388
2008
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-
1
-
2
1
-
4
-
1
1
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1
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1
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1
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1
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3
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1
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1
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2
1
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4
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1
1
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1
-
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-
1
-
-
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-
3
-
1
-
-
-
-
-
-
3
3
722955
Rea
Structure and mechanism of Hpc ...
Escherichia coli
J. Mol. Biol.
373
866-876
2007
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1
1
-
-
-
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-
-
1
1
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2
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1
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1
1
2
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1
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1
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1
1
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1
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1
1
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1
1
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-
721601
Wang
Purification and biochemical c ...
Escherichia coli
Biochemistry
44
9447-9455
2005
-
-
1
-
1
-
2
6
-
9
1
1
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1
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1
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5
-
1
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3
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2
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1
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1
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2
2
6
-
9
1
1
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1
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5
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3
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1
1
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3
3