EC Number   |
General Information |
Reference |
|---|
    3.1.4.46 | evolution |
phylogenetic analysis, overview |
-, 729721 |
| 3.1.4.46 | evolution |
phylogenetic analysis, overview. A common feature of this enzyme family is the presence of the classical triosephosphate isomerase barrel fold |
729721 |
| 3.1.4.46 | evolution |
phylogenetic analysis, overview. Escherichia coli GlpQ and UgpQ possess a significant similarity, suggesting a common evolutionary origin |
729721 |
| 3.1.4.46 | evolution |
phylogenetic analysis, overview. PfGDPD shows clear homology with bacterial GP-PDEs |
729721 |
| 3.1.4.46 | evolution |
phylogenetic analysis, overview. The enzyme Pgc1p belongs to the superfamily of phospholipase-C-like enzymes |
729721 |
| 3.1.4.46 | evolution |
phylogenetic analysis, overview. The enzyme shows a structure unusual for the enzyme family, the T2047enzyme of Agrobacterium tumefaciens forms a hexamer and, in particular, a trimer of dimers, with a channel passing through the center of the assembly |
729721 |
| 3.1.4.46 | evolution |
phylogenetic analysis, overview. The phosphodiesterase GpdQ is unrelated to the Escherichia coli enzyme UgpQ. The crystal structure of GpdQ emphasizes its difference compared to all other bacterial GP-PDEs with respect to the absence of the conserved triosephosphate isomerase barrel fold in the catalytic site. GpdQ is clustered separately in the phylogenetic tree and appears as a structurally distinct GP-PDE, its secondary structure prediction suggests that it more properly belongs to the alpha/beta-sandwich metallo-dependent phosphoesterase family |
729721 |
| 3.1.4.46 | evolution |
the human glycerophosphodiester phosphodiesterase domain (GDPD) containing family consists of 5 isozymes, GDPD1-5 |
730482 |
| 3.1.4.46 | malfunction |
ablating GDE2 expression in the spinal cord using small-interfering RNAs results in the loss of post-mitotic motor neurons and an increase in cell death |
729721 |
| 3.1.4.46 | malfunction |
abrogation of nontypeable Haemophilus influenzae protein D function reduces phosphorylcholine decoration, adherence to airway epithelial A549 cells, and fitness in a chinchilla, Chinchilla lanigera, model of otitis media. Exposure of NTHI to antibodies directed against the vaccine formulation recapitulates the phosphorylcholine decoration and NTHI adherence phenotypes exhibite by PD/GlpQ-deficient NTHI, mechanism(s) of anti-PD/GlpQ antibody-mediated protection from NTHI-induced otitis media, overview |
-, 716983 |
