Substrates: the bifunctional enzyme PmdF shows obvious aldolase activity when 4-carboxy-4-hydroxy-2-oxoadipate is used as substrate and obvious oxalacetate decarboxylase activity when oxaloacetate is used as substrate Products: -
Substrates: the bifunctional enzyme PmdF shows obvious aldolase activity when 4-carboxy-4-hydroxy-2-oxoadipate is used as substrate and obvious oxalacetate decarboxylase activity when oxaloacetate is used as substrate Products: -
Substrates: 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 Products: -
Substrates: the bifunctional enzyme PmdF shows obvious aldolase activity when 4-carboxy-4-hydroxy-2-oxoadipate is used as substrate and obvious oxalacetate decarboxylase activity when oxaloacetate is used as substrate Products: -
Substrates: the bifunctional enzyme PmdF shows obvious aldolase activity when 4-carboxy-4-hydroxy-2-oxoadipate is used as substrate and obvious oxalacetate decarboxylase activity when oxaloacetate is used as substrate Products: -
Substrates: 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 Products: -
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
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
the protocatechuate 4,5-cleavage pathway is mainly distributed in alpha- and beta-proteobacteria, gene clusters of protocatechuate 4,5-cleavage pathway in strain CNB-1 and other bacterial strains, genotyping and phylogenetic analysis, overview. Two types of genetic organization/cluster are recognized for PCA 4,5-cleavage pathway: The Sphingobium-type gene cluster constitutes several transcriptional units. The Comamonas-Pseudomonas type constitutes only one transcriptional unit
the protocatechuate 4,5-cleavage pathway is mainly distributed in alpha- and beta-proteobacteria, gene clusters of protocatechuate 4,5-cleavage pathway in strain CNB-1 and other bacterial strains, genotyping and phylogenetic analysis, overview. Two types of genetic organization/cluster are recognized for PCA 4,5-cleavage pathway: The Sphingobium-type gene cluster constitutes several transcriptional units. The Comamonas-Pseudomonas type constitutes only one transcriptional unit
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
the enzyme catalyzes the last step of the protocatechuate 4,5-cleavage pathway. Vanillate, 3-hydroxybenzoate, and 4-hydroxybenzoate are degraded via protocatechuate 4,5-cleavage pathway
the enzyme catalyzes the last step of the protocatechuate 4,5-cleavage pathway. Vanillate, 3-hydroxybenzoate, and 4-hydroxybenzoate are degraded via protocatechuate 4,5-cleavage pathway
site-directed mutagenesis, the mutant shows reduced 4-hydroxy-4-methyl-2-oxoglutarate aldolase and oxaloacetate decarboxylase activities compared to the wild-type enzyme
gene pmdF, orf CtCNB1_2744, DNA and amino acid sequence determination and analysis, genetic organization, phylogenetic analysis, expression in Escherichia coli
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
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