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Literature summary for 4.1.3.B3 extracted from

  • 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 (2014), Biochemistry, 53, 542-553.
    View publication on PubMed
Search for more literature for 4.1.3.B3

Protein Variants

Protein Variants Comment Organism
E199A site-directed mutagenesis, the mutant shows reduced 4-hydroxy-4-methyl-2-oxoglutarate aldolase and oxaloacetate decarboxylase activities compared to the wild-type enzyme Pseudomonas putida

Inhibitors

Inhibitors Comment Organism Structure
oxalate competitive inhibition Pseudomonas putida

Metals/Ions

Metals/Ions Comment Organism Structure
Co2+ required Pseudomonas putida
Mg2+ a magnesium ion is coordinated directly or indirectly via water through interactions with Asp102, Asp124, and Glu199 Pseudomonas putida
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 Pseudomonas putida

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
4-carboxy-4-hydroxy-2-oxoadipate Pseudomonas putida
-
 oxaloacetate + pyruvate
-
 ?
additional information Pseudomonas putida 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. EC 4.1.3.17. 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 ?
-
 ?

Organism

Organism UniProt Comment Textmining
Pseudomonas putida A5W059
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
4-carboxy-4-hydroxy-2-oxoadipate
-
 Pseudomonas putida oxaloacetate + pyruvate
-
 ?
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. EC 4.1.3.17. 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 Pseudomonas putida ?
-
 ?

Subunits

Subunits Comment Organism
trimer
-
 Pseudomonas putida

Synonyms

Synonyms Comment Organism
4-hydroxy-4-methyl-2-oxoglutarate/4-carboxy-4-hydroxy-2-oxoadipate aldolase
-
 Pseudomonas putida
CHA aldolase
-
 Pseudomonas putida
HMG/CHA aldolase
-
 Pseudomonas putida

General Information

General Information Comment Organism
evolution structural and functional relationships of the HMG/CHA aldolase and RraA-like proteins, overview Pseudomonas putida
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. The enzyme catalyzes the final step Pseudomonas putida
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 Pseudomonas putida