EC Number   |
General Information |
Reference |
|---|
  4.1.3.B3 | evolution |
structural and functional relationships of the HMG/CHA aldolase and RraA-like proteins, overview |
727049 |
| 4.1.3.B3 | evolution |
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 |
-, 726779 |
| 4.1.3.B3 | 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 |
727049 |
| 4.1.3.B3 | metabolism |
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 |
-, 726779 |
| 4.1.3.B3 | more |
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 |
727049 |
