EC Number   |
General Information |
Reference |
|---|
    4.1.3.17 | evolution |
RNase E activity A, RraA, like protein (RraA-like protein) TtRraA from Thermus thermophilus HB8 (TtRraA) contains HMG aldolase and oxaloacetate decarboxylase activities. The enzyme TtRraA contains a G-X20-R-D-X2-E/D motif |
-, 727049 |
| 4.1.3.17 | evolution |
RNase E activity A, RraA, like proteins TtRraA and Yer010Cp from Thermus thermophilus HB8 (TtRraA) and Saccharomyces cerevisiae S288C (Yer010Cp) contain HMG aldolase and oxaloacetate decarboxylase activities and a G-X20-R-D-X2-E/D motif, that may support metal binding. The Pseudomonas putida F1 HMG/CHA aldolase has a D-X20-R-D motif. Structural and fucntional relationships of the HMG/CHA aldolase and RraA-like proteins, overview |
727049 |
| 4.1.3.17 | evolution |
RNase E activity A-like protein (RraA-like protein) Yer010Cp from Saccharomyces cerevisiae S288C contains HMG aldolase and oxaloacetate decarboxylase activities. The enzyme Yer010Cp contains a G-X20-R-D-X2-E/D motif |
727049 |
| 4.1.3.17 | 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 |
727049 |
| 4.1.3.17 | 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 |
