4.1.3.B3: 4-carboxy-4-hydroxy-2-oxoadipate aldolase

This is an abbreviated version!
For detailed information about 4-carboxy-4-hydroxy-2-oxoadipate aldolase, go to the full flat file.

Reaction

Synonyms

4-carboxy-4-hydroxy-2-oxoadipate aldolase/oxaloacetate decarboxylase, 4-hydroxy-4-methyl-2-oxoglutarate/4-carboxy-4-hydroxy-2-oxoadipate aldolase, CHA aldolase, HMG/CHA aldolase, PmdF

ECTree

4 Lyases

4.1 Carbon-carbon lyases

4.1.3 Oxo-acid-lyases

4.1.3.B3 4-carboxy-4-hydroxy-2-oxoadipate aldolase

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Results	in table
2	AA Sequence
2	Cloned(Commentary)
1	Crystallization (Commentary)
7	General Information
1	Inhibitors
2	kcat/KM [mM/s]
2	KM Value [mM]
4	Metals/Ions
1	Molecular Weight [Da]
6	Natural Substrates/ Products (Substrates)
4	Organism
5	Protein Variants
2	Purification (Commentary)
1	Reaction
4	Reference
2	Source Tissue
1	Specific Activity [micromol/min/mg]
1	Storage Stability
7	Substrates and Products (Substrate)
2	Subunits
9	Synonyms
1	Systematic Name
1	Temperature Optimum [°C]
2	Turnover Number [1/s]

General Information

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General Information on EC 4.1.3.B3 - 4-carboxy-4-hydroxy-2-oxoadipate aldolase

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evolution

3 entries

metabolism

3 entries

additional information

Pseudomonas putida

A5W059

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

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