EC Number   |
General Information |
Reference |
|---|
   3.7.1.24 | evolution |
both phloretin hydrolase, EC 3.7.1.4, and 2,4-diacetylphloroglucinol hydrolase show no sequence similarity to other known C-C hydrolase enzymes and contain no motifs typical of the alpha/beta-hydrolase-fold superfamily |
-, 733155 |
| 3.7.1.24 | evolution |
the amino acid sequence of PhlG displays 25-37% sequence identity to several hypothetical proteins and the phloretin hydrolase (EC 3.7.1.4) from Eubacterium ramulus. Neither PhlG nor phloretin hydrolase possess sequence homology to other C-C bond-cleaving hydrolases or motifs typical of the alpha/beta hydrolase family, suggesting these two enzymes belong to a distinct hydrolase family, the enzyme structure with a Bet v1-like fold also distinguishes PhlG from the classical alpha/beta-fold hydrolases. PhlG is a hydrolase whose catalytic domain belongs to the Bet v1-like fold and belongs to another family within the Bet v1-like superfamily. The most important characteristic of Bet v1-like proteins is the presence of an interior hydrophobic/amphiphilic pocket accessible to the exterior, present in the C-terminal domain of PhlG |
-, 734165 |
| 3.7.1.24 | evolution |
the C-C hydrolase enzyme exhibits a Bet v1-like fold rather than the alpha/beta hydrolase fold common to C-C hydrolases |
735304 |
| 3.7.1.24 | evolution |
the PhlG protein from Mycobacterium abscessus 103 (mPhlG), which shares 30% sequence identity with phloretin hydrolase from Eubacterium ramulus and 38% sequence identity with 2,4-diacetylphloroglucinol hydrolase from Pseudomonas fluorescens Pf-5, is a putative carbon-carbon bond hydrolase |
-, 733038 |
| 3.7.1.24 | malfunction |
2,4-diacetylphloroglucinol added to cultures of a DAPG-negative DELTAphlA mutant of strain CHA0 is completely degraded, and MAPG is temporarily accumulated. In contrast, 2,4-diacetylphloroglucinol is not degraded in cultures of a DELTAphlA/DELTAphlG double mutant |
-, 733155 |
| 3.7.1.24 | malfunction |
mutation of His123, His251, Glu154 and Glu255 (conserved zinc binding residues) results in variants that are either poorly expressed, or of much reduced activity. Mutation of Tyr115 and His203, thought to bind the phenol groups in the 1-and 3-positions of the phloroglucinol ring respectively, results in variants of 15fold reduced activity and an inactive variant |
735304 |
| 3.7.1.24 | metabolism |
2,4-diacetylphloroglucinol is produced as an antifungal compound by the plant-root associated bacterium |
-, 734589 |
| 3.7.1.24 | metabolism |
the potent antimicrobial compound 2,4-diacetylphloroglucinol is a major determinant of biocontrol activity of plant-beneficial Pseudomonas fluorescens CHA0 against root diseases caused by fungal pathogens |
-, 733155 |
| 3.7.1.24 | more |
the enzyme structure, PDB ID 3HWP, is used for a homology model of phloretin hydrolase, Phy, EC 3.7.1.4, from Eubacterium ramulus. Active site structure of the enzyme Phlg, overview |
735304 |
| 3.7.1.24 | more |
three-dimensional structure analysis: the overall structure includes a small N-terminal domain mainly involved in dimerization and a C-terminal domain of Bet v1-like fold, which distinguishes enzyme PhlG from the classical alpha/beta-fold hydrolases. A dumbbell-shaped substrate access tunnel was identified to connect a narrow interior amphiphilic pocket to the exterior solvent. The tunnel is likely to undergo a significant conformational change upon substrate binding to the active site, computational docking studies |
-, 734165 |
