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2,4-diacetylphloroglucinol + H2O = 2-acetylphloroglucinol + acetate
2,4-diacetylphloroglucinol + H2O = 2-acetylphloroglucinol + acetate
catalytic reaction mechanism, overview. A water molecule, bound by the zinc, is responsible for initiating the CC bond cleavage reaction through nucleophilic attack at the acyl carbonyl carbon atom
2,4-diacetylphloroglucinol + H2O = 2-acetylphloroglucinol + acetate
cleavage of the 2,4-diacetylphloroglucinol C-C bond proceeds via nucleophilic attack by a water molecule, which is coordinated by a zinc ion. Residues Tyr121, Tyr229, and Asn132, which are predicted to be hydrogen-bonded to the hydroxyl groups and unhydrolyzed acetyl group, can finely tune and position the bound substrate in a reactive orientation, catalytic reaction mechanism, overview
2,4-diacetylphloroglucinol + H2O = 2-acetylphloroglucinol + acetate
cleavage of the 2,4-diacetylphloroglucinol C-C bond proceeds via nucleophilic attack by a water molecule, which is coordinated by a zinc ion. Residues Tyr121, Tyr229, and Asn132, which are predicted to be hydrogen-bonded to the hydroxyl groups and unhydrolyzed acetyl group, can finely tune and position the bound substrate in a reactive orientation, catalytic reaction mechanism, overview
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2,4-diacetylphloroglucinol + H2O = 2-acetylphloroglucinol + acetate
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2,4-diacetylphloroglucinol + H2O
2-acetylphloroglucinol + acetate
additional information
?
-
2,4-diacetylphloroglucinol + H2O
2-acetylphloroglucinol + acetate
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-
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?
2,4-diacetylphloroglucinol + H2O
2-acetylphloroglucinol + acetate
2,4-diacetylphloroglucinol i.e. 1,1'-(2,4,6-trihydroxybenzene-1,3-diyl)diethan-1-one
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-
?
2,4-diacetylphloroglucinol + H2O
2-acetylphloroglucinol + acetate
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-
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?
2,4-diacetylphloroglucinol + H2O
2-acetylphloroglucinol + acetate
2,4-diacetylphloroglucinol i.e. 1,1'-(2,4,6-trihydroxybenzene-1,3-diyl)diethan-1-one
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?
2,4-diacetylphloroglucinol + H2O
2-acetylphloroglucinol + acetate
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-
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?
2,4-diacetylphloroglucinol + H2O
2-acetylphloroglucinol + acetate
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-
-
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?
2,4-diacetylphloroglucinol + H2O
2-acetylphloroglucinol + acetate
-
-
-
?
2,4-diacetylphloroglucinol + H2O
2-acetylphloroglucinol + acetate
-
-
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?
2,4-diacetylphloroglucinol + H2O
2-acetylphloroglucinol + acetate
-
-
-
?
2,4-diacetylphloroglucinol + H2O
2-acetylphloroglucinol + acetate
the enzyme functions as a hydrolase specifically degrades 2,4-diacetylphloroglucinol, DAPG, to equimolar amounts of mildly toxic monoacetylphloroglucinol (MAPG) and acetate
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?
2,4-diacetylphloroglucinol + H2O
2-acetylphloroglucinol + acetate
2,4-diacetylphloroglucinol hydrolase catalyzes hydrolytic C-C bond cleavage, cleaving one of the C-C bonds linking the acetyl groups to the phenolic ring, of the antibiotic 2,4-diacetylphloroglucinol to form monoacetylphloroglucinol, a rare class of reactions in chemistry and biochemistry, strict substrate specificity, no degradation of other compounds of similar structure such as monoacetylphloroglucinol and triacetylphloroglucinol
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?
2,4-diacetylphloroglucinol + H2O
2-acetylphloroglucinol + acetate
modeling of a theoretical transition state for the substrate hydrolysis into the active site revealing that a water molecule, bound by the zinc, can be responsible for initiating the C-C bond cleavage reaction through nucleophilic attack at the acyl carbonyl carbon atom. Residue Asn132 in Phlg is thought to make a hydrogen bond to the acyl group of the native substrate in the enzyme. Tyr121 is thought to hydrogen bond to the phenol group in the 1-position of the aromatic ring between the two acetyl groups in the substrate
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?
2,4-diacetylphloroglucinol + H2O
2-acetylphloroglucinol + acetate
degradation of 2,4-diacetylphloroglucinol catalyzed by PhlG plays an insignificant role in 2,4-diacetylphloroglucinol tolerance but contributes to bacterial growth advantages under carbon/nitrogen starvation conditions
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?
2,4-diacetylphloroglucinol + H2O
2-acetylphloroglucinol + acetate
-
-
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?
2,4-diacetylphloroglucinol + H2O
2-acetylphloroglucinol + acetate
-
-
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?
2,4-diacetylphloroglucinol + H2O
2-acetylphloroglucinol + acetate
degradation of 2,4-diacetylphloroglucinol catalyzed by PhlG plays an insignificant role in 2,4-diacetylphloroglucinol tolerance but contributes to bacterial growth advantages under carbon/nitrogen starvation conditions
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?
2,4-diacetylphloroglucinol + H2O
2-acetylphloroglucinol + acetate
-
-
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?
2,4-diacetylphloroglucinol + H2O
2-acetylphloroglucinol + acetate
-
-
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?
2,4-diacetylphloroglucinol + H2O
2-acetylphloroglucinol + acetate
the enzyme functions as a hydrolase specifically degrades 2,4-diacetylphloroglucinol, DAPG, to equimolar amounts of mildly toxic monoacetylphloroglucinol (MAPG) and acetate
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?
2,4-diacetylphloroglucinol + H2O
2-acetylphloroglucinol + acetate
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-
-
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?
2,4-diacetylphloroglucinol + H2O
2-acetylphloroglucinol + acetate
-
-
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?
2,4-diacetylphloroglucinol + H2O
2-acetylphloroglucinol + acetate
2,4-diacetylphloroglucinol hydrolase catalyzes hydrolytic C-C bond cleavage, cleaving one of the C-C bonds linking the acetyl groups to the phenolic ring, of the antibiotic 2,4-diacetylphloroglucinol to form monoacetylphloroglucinol, a rare class of reactions in chemistry and biochemistry, strict substrate specificity, no degradation of other compounds of similar structure such as monoacetylphloroglucinol and triacetylphloroglucinol
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2,4-diacetylphloroglucinol + H2O
2-acetylphloroglucinol + acetate
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?
additional information
?
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the PhlG enzyme does not degrade other compounds with structures similar to diacetylphloroglucinol, such as monoacetylphloroglucinol and triacetylphloroglucinol, or salicylate, and 2,6-dihydroxyacetophenone, suggesting strict substrate specificity
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?
additional information
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the PhlG enzyme does not degrade other compounds with structures similar to diacetylphloroglucinol, such as monoacetylphloroglucinol and triacetylphloroglucinol, or salicylate, and 2,6-dihydroxyacetophenone, suggesting strict substrate specificity
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?
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2,4-diacetylphloroglucinol + H2O
2-acetylphloroglucinol + acetate
2,4-diacetylphloroglucinol + H2O
2-acetylphloroglucinol + acetate
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-
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?
2,4-diacetylphloroglucinol + H2O
2-acetylphloroglucinol + acetate
-
-
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?
2,4-diacetylphloroglucinol + H2O
2-acetylphloroglucinol + acetate
-
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?
2,4-diacetylphloroglucinol + H2O
2-acetylphloroglucinol + acetate
-
-
-
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?
2,4-diacetylphloroglucinol + H2O
2-acetylphloroglucinol + acetate
-
-
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?
2,4-diacetylphloroglucinol + H2O
2-acetylphloroglucinol + acetate
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?
2,4-diacetylphloroglucinol + H2O
2-acetylphloroglucinol + acetate
the enzyme functions as a hydrolase specifically degrades 2,4-diacetylphloroglucinol, DAPG, to equimolar amounts of mildly toxic monoacetylphloroglucinol (MAPG) and acetate
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?
2,4-diacetylphloroglucinol + H2O
2-acetylphloroglucinol + acetate
degradation of 2,4-diacetylphloroglucinol catalyzed by PhlG plays an insignificant role in 2,4-diacetylphloroglucinol tolerance but contributes to bacterial growth advantages under carbon/nitrogen starvation conditions
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?
2,4-diacetylphloroglucinol + H2O
2-acetylphloroglucinol + acetate
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?
2,4-diacetylphloroglucinol + H2O
2-acetylphloroglucinol + acetate
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-
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?
2,4-diacetylphloroglucinol + H2O
2-acetylphloroglucinol + acetate
degradation of 2,4-diacetylphloroglucinol catalyzed by PhlG plays an insignificant role in 2,4-diacetylphloroglucinol tolerance but contributes to bacterial growth advantages under carbon/nitrogen starvation conditions
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?
2,4-diacetylphloroglucinol + H2O
2-acetylphloroglucinol + acetate
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?
2,4-diacetylphloroglucinol + H2O
2-acetylphloroglucinol + acetate
the enzyme functions as a hydrolase specifically degrades 2,4-diacetylphloroglucinol, DAPG, to equimolar amounts of mildly toxic monoacetylphloroglucinol (MAPG) and acetate
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?
2,4-diacetylphloroglucinol + H2O
2-acetylphloroglucinol + acetate
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?
2,4-diacetylphloroglucinol + H2O
2-acetylphloroglucinol + acetate
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?
2,4-diacetylphloroglucinol + H2O
2-acetylphloroglucinol + acetate
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?
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Co2+
specifically and significantly activates the enzyme, shows a hyperbolic saturation curve in the micromolar range, binding to the enzyme might induce a conformational change that increases the catalytic effect of Zn2+ or might forma a distinct catalytic site besides that for Zn2+
Zn2+
dependent on
Zn2+
a Zn-dependent C-C hydrolase, bound in the active site, chelated by four amino acid side-chains, His270, His129, Glu274 and Glu160, might also have structural role in Phlg
Zn2+
a Zn-dependent C-C hydrolase, the metal ion may play an essential role in catalysis and is identified as bound inside the hydrophobic/amphiphilic pocket, coordinated by His129(beta5), Glu160(beta6), His270(alpha10), Glu274(alpha10), and a water molecule with pentagonal bipyramidal coordination geometry. It may play an important structural role in stabilizing the PhlG catalytic domain by holding the strands beta5 and beta6 and the helix alpha10 together
Zn2+
a zinc hydrolase, located at the bottom of a deep narrow pocket of the enzyme molecule, coordinated by H129, E160, H270, and E274
additional information
the enzyme has a 168HXHXD172 metal binding motif. Poor effects on enzyme activity by Ca2+, Ni2+, Fe3+, Zn2+, and Mg2+
additional information
-
the enzyme has a 168HXHXD172 metal binding motif. Poor effects on enzyme activity by Ca2+, Ni2+, Fe3+, Zn2+, and Mg2+
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0.024 - 0.873
2,4-diacetylphloroglucinol
0.024
2,4-diacetylphloroglucinol
recombinant enzyme, pH 7.0, 25°C
0.041
2,4-diacetylphloroglucinol
recombinant mutant E160A, pH 7.1, 25°C
0.042
2,4-diacetylphloroglucinol
recombinant mutant E274A, pH 7.1, 25°C
0.14
2,4-diacetylphloroglucinol
recombinant enzyme, pH 7.0, 30°C
0.18
2,4-diacetylphloroglucinol
recombinant mutant H214Q, pH 7.1, 25°C
0.242
2,4-diacetylphloroglucinol
recombinant mutant Y121A, pH 7.1, 25°C
0.268
2,4-diacetylphloroglucinol
recombinant mutant Y229F, pH 7.1, 25°C
0.272
2,4-diacetylphloroglucinol
recombinant wild-type enzyme, pH 7.1, 25°C
0.32
2,4-diacetylphloroglucinol
recombinant mutant H214A, pH 7.1, 25°C
0.61
2,4-diacetylphloroglucinol
recombinant mutant N132A, pH 7.1, 25°C
0.873
2,4-diacetylphloroglucinol
recombinant mutant Y229A, pH 7.1, 25°C
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0.000026 - 33
2,4-diacetylphloroglucinol
0.000026
2,4-diacetylphloroglucinol
recombinant mutant E274A, pH 7.1, 25°C
0.000081
2,4-diacetylphloroglucinol
recombinant mutant E160A, pH 7.1, 25°C
0.05
2,4-diacetylphloroglucinol
recombinant mutant Y121A, pH 7.1, 25°C
0.21
2,4-diacetylphloroglucinol
recombinant mutant Y229A, pH 7.1, 25°C
0.58
2,4-diacetylphloroglucinol
recombinant mutant H214Q, pH 7.1, 25°C
0.74
2,4-diacetylphloroglucinol
recombinant mutant N132A, pH 7.1, 25°C
1.4
2,4-diacetylphloroglucinol
recombinant mutants Y229F and H214A, pH 7.1, 25°C
4.7
2,4-diacetylphloroglucinol
recombinant wild-type enzyme, pH 7.1, 25°C
5.8
2,4-diacetylphloroglucinol
recombinant enzyme, pH 7.0, 25°C
33
2,4-diacetylphloroglucinol
recombinant enzyme, pH 7.0, 30°C
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0.00062 - 17
2,4-diacetylphloroglucinol
0.00062
2,4-diacetylphloroglucinol
recombinant mutant E274A, pH 7.1, 25°C
0.002
2,4-diacetylphloroglucinol
recombinant mutant E160A, pH 7.1, 25°C
0.21
2,4-diacetylphloroglucinol
recombinant mutant Y121A, pH 7.1, 25°C
1.1
2,4-diacetylphloroglucinol
recombinant mutant Y229A, pH 7.1, 25°C
1.2
2,4-diacetylphloroglucinol
recombinant mutant N132A, pH 7.1, 25°C
3.3
2,4-diacetylphloroglucinol
recombinant mutant H214Q, pH 7.1, 25°C
4.3
2,4-diacetylphloroglucinol
recombinant mutant H214A, pH 7.1, 25°C
5.2
2,4-diacetylphloroglucinol
recombinant mutant Y229F, pH 7.1, 25°C
17
2,4-diacetylphloroglucinol
recombinant wild-type enzyme, pH 7.1, 25°C
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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
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
evolution
the C-C hydrolase enzyme exhibits a Bet v1-like fold rather than the alpha/beta hydrolase fold common to C-C hydrolases
evolution
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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
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
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evolution
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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
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evolution
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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
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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
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
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
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metabolism
2,4-diacetylphloroglucinol is produced as an antifungal compound by the plant-root associated bacterium
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
metabolism
-
2,4-diacetylphloroglucinol is produced as an antifungal compound by the plant-root associated bacterium
-
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
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physiological function
2,4-diacetylphloroglucinol is produced by Pseudomonas fluorescens an antibiotic that represses the growth of pathogenic microorganisms in the rhizosphere of host plants, the diacetylphloroglucinol hydrolase is a key compound in the biocontrol of Pseudomonas fluorescens
physiological function
the hydrolase is required for specific degradation of the antifungal compound 2,4-diacetylphloroglucinol in the biocontrol agent Pseudomonas fluorescens CHA0, it catalyzes the conversion of the potent antibiotic DAPG to less-toxic MAPG, with a high specificity for its substrate
physiological function
-
enzymatic production of the antifungal compound 2,4-diacetylphloroglucinol inhibits the growth of Fusarium oxysporum f. sp. lycopersici, and controls Fusarium wilt of tomato caused by Fusarium oxysporum f. sp. lycopersici
physiological function
the enzyme contributes to bacterial growth advantages under carbon/nitrogen starvation conditions
physiological function
OmpR negatively influences the intracellular concentrations of 2,4-diacetylphloroglucinol by regulating the transcriptional activity of the hydrolase phlG in Pseudomonas fluorescens 2P24
physiological function
the pathway-specific regulator PhlH modulates 2,4-diacetylphloroglucinol levels by controlling the expression of 2,4-diacetylphloroglucinol hydrolase PhlG in response to 2,4-diacetylphloroglucinol and monoacetylphloroglucinol. Since 2,4-diacetylphloroglucinol biosynthesis imposes a metabolic burden on biocontrol pseudomonads, it is expected that the fine regulation of phlG by PhlH offers a way to dynamically modulate the metabolic loads attributed to 2,4-diacetylphloroglucinol production
physiological function
-
enzymatic production of the antifungal compound 2,4-diacetylphloroglucinol inhibits the growth of Fusarium oxysporum f. sp. lycopersici, and controls Fusarium wilt of tomato caused by Fusarium oxysporum f. sp. lycopersici
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physiological function
-
the enzyme contributes to bacterial growth advantages under carbon/nitrogen starvation conditions
-
physiological function
-
the pathway-specific regulator PhlH modulates 2,4-diacetylphloroglucinol levels by controlling the expression of 2,4-diacetylphloroglucinol hydrolase PhlG in response to 2,4-diacetylphloroglucinol and monoacetylphloroglucinol. Since 2,4-diacetylphloroglucinol biosynthesis imposes a metabolic burden on biocontrol pseudomonads, it is expected that the fine regulation of phlG by PhlH offers a way to dynamically modulate the metabolic loads attributed to 2,4-diacetylphloroglucinol production
-
physiological function
-
OmpR negatively influences the intracellular concentrations of 2,4-diacetylphloroglucinol by regulating the transcriptional activity of the hydrolase phlG in Pseudomonas fluorescens 2P24
-
physiological function
-
the hydrolase is required for specific degradation of the antifungal compound 2,4-diacetylphloroglucinol in the biocontrol agent Pseudomonas fluorescens CHA0, it catalyzes the conversion of the potent antibiotic DAPG to less-toxic MAPG, with a high specificity for its substrate
-
additional information
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
additional information
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
additional information
-
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
additional information
-
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
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H214Q
site-directed mutagenesis, mutation of a polar residue that is predicted to form hydrogen bond with the polar groups of the substrate, the mutant shows reduced activity compared to the wild-type enzyme
N132A
site-directed mutagenesis, mutation of a polar residue that is predicted to form hydrogen bond with the polar groups of the substrate, the mutant shows reduced activity compared to the wild-type enzyme
Y229A
site-directed mutagenesis, mutation of a polar residue that is predicted to form hydrogen bond with the polar groups of the substrate, the mutant shows reduced activity compared to the wild-type enzyme
Y229F
site-directed mutagenesis, mutation of a polar residue that is predicted to form hydrogen bond with the polar groups of the substrate, the mutant shows reduced activity compared to the wild-type enzyme
E160A
-
site-directed mutagenesis, the mutation of the zinc binding residue leads to reduced activity compared to the wild-type enzyme
-
E274A
-
site-directed mutagenesis, the mutation of the zinc binding residue leads to reduced activity compared to the wild-type enzyme
-
H214A
-
site-directed mutagenesis, mutation of a polar residue that is predicted to form hydrogen bond with the polar groups of the substrate, the mutant shows reduced activity compared to the wild-type enzyme
-
Y121A
-
site-directed mutagenesis, mutation of a polar residue that is predicted to form hydrogen bond with the polar groups of the substrate, the mutant shows reduced activity compared to the wild-type enzyme
-
Y229F
-
site-directed mutagenesis, mutation of a polar residue that is predicted to form hydrogen bond with the polar groups of the substrate, the mutant shows reduced activity compared to the wild-type enzyme
-
E160A
site-directed mutagenesis, almost inactive enzyme
E160A
site-directed mutagenesis, the mutation of the zinc binding residue leads to reduced activity compared to the wild-type enzyme
E274A
site-directed mutagenesis, a mutant of very low activity
E274A
site-directed mutagenesis, the mutation of the zinc binding residue leads to reduced activity compared to the wild-type enzyme
H214A
site-directed mutagenesis, mutation of a polar residue that is predicted to form hydrogen bond with the polar groups of the substrate, the mutant shows reduced activity compared to the wild-type enzyme
H214A
site-directed mutagenesis, the mutant shows an unaltered KM but reduced catalytic efficiency with diacetyl phloroglucinol compared to the wild-type
H270A
site-directed mutagenesis, inactive mutant
H270A
site-directed mutagenesis, inactive enzyme
Y121A
site-directed mutagenesis, mutation of a polar residue that is predicted to form hydrogen bond with the polar groups of the substrate, the mutant shows reduced activity compared to the wild-type enzyme
Y121A
site-directed mutagenesis, the mutant shows reduced KM and catalytic efficiency with diacetyl phloroglucinol compared to the wild-type
additional information
construction of the DELTAphlG mutant CHA1091 and DELTAphlA/DELTAphlG double mutant
additional information
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
additional information
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construction of the DELTAphlG mutant CHA1091 and DELTAphlA/DELTAphlG double mutant
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at 8 h after inoculation, 0.1 mM 2,4-diacetylphloroglucinol has an about 8fold induction of enzyme expression, whereas 0.1 mM monoacetylphloroglucinol has about 2fold induction of enzyme expression
expression of gene phlG is not influenced by the substrate 2,4-diacetylphloroglucinol or the degradation product monoacetylphloroglucinol but is subject to positive control by the GacS/GacA two-component system and to negative control by the pathway-specific regulators PhlF and PhlH
gene phlG expression regulation study, overview
OmpR negatively influences the intracellular concentrations of 2,4-diacetylphloroglucinol by regulating the transcriptional activity of the hydrolase phlG in Pseudomonas fluorescens 2P24
the pathway-specific regulator PhlH represses the phlG gene expression in vivo.Repressed expression of phlG is dependent on the interaction between PhlH and the palindromic sequence within the phlG promoter region
the transcriptional regulator OmpR up-regulates the transcriptional activity of the enzyme
the transcriptional regulator PhlH represses the expression of the enzyme
at 8 h after inoculation, 0.1 mM 2,4-diacetylphloroglucinol has an about 8fold induction of enzyme expression, whereas 0.1 mM monoacetylphloroglucinol has about 2fold induction of enzyme expression
at 8 h after inoculation, 0.1 mM 2,4-diacetylphloroglucinol has an about 8fold induction of enzyme expression, whereas 0.1 mM monoacetylphloroglucinol has about 2fold induction of enzyme expression
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expression of gene phlG is not influenced by the substrate 2,4-diacetylphloroglucinol or the degradation product monoacetylphloroglucinol but is subject to positive control by the GacS/GacA two-component system and to negative control by the pathway-specific regulators PhlF and PhlH
expression of gene phlG is not influenced by the substrate 2,4-diacetylphloroglucinol or the degradation product monoacetylphloroglucinol but is subject to positive control by the GacS/GacA two-component system and to negative control by the pathway-specific regulators PhlF and PhlH
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-
gene phlG expression regulation study, overview
gene phlG expression regulation study, overview
-
-
OmpR negatively influences the intracellular concentrations of 2,4-diacetylphloroglucinol by regulating the transcriptional activity of the hydrolase phlG in Pseudomonas fluorescens 2P24
OmpR negatively influences the intracellular concentrations of 2,4-diacetylphloroglucinol by regulating the transcriptional activity of the hydrolase phlG in Pseudomonas fluorescens 2P24
-
-
the pathway-specific regulator PhlH represses the phlG gene expression in vivo.Repressed expression of phlG is dependent on the interaction between PhlH and the palindromic sequence within the phlG promoter region
the pathway-specific regulator PhlH represses the phlG gene expression in vivo.Repressed expression of phlG is dependent on the interaction between PhlH and the palindromic sequence within the phlG promoter region
-
-
the transcriptional regulator OmpR up-regulates the transcriptional activity of the enzyme
the transcriptional regulator OmpR up-regulates the transcriptional activity of the enzyme
-
-
the transcriptional regulator PhlH represses the expression of the enzyme
the transcriptional regulator PhlH represses the expression of the enzyme
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Zhang, Z.; Jiang, Y.L.; Wu, Y.; He, Y.X.
Crystallization and preliminary X-ray diffraction analysis of a putative carbon-carbon bond hydrolase from Mycobacterium abscessus 103
Acta Crystallogr. Sect. F
71
239-242
2015
Mycobacteroides abscessus, Mycobacteroides abscessus 103
brenda
Bottiglieri, M.; Keel, C.
Characterization of PhlG, a hydrolase that specifically degrades the antifungal compound 2,4-diacetylphloroglucinol in the biocontrol agent Pseudomonas fluorescens CHA0
Appl. Environ. Microbiol.
72
418-427
2006
Pseudomonas fluorescens (A0A2C9EVE6), Pseudomonas fluorescens CHA0 (A0A2C9EVE6)
brenda
Saitou, H.; Watanabe, M.; Maruyama, K.
Molecular and catalytic properties of 2,4-diacetylphloroglucinol hydrolase (PhlG) from Pseudomonas sp. YGJ3
Biosci. Biotechnol. Biochem.
76
1239-1241
2012
Pseudomonas sp. (F7J5X9), Pseudomonas sp.
brenda
He, Y.-X.; Huang, l.; Xue, Y.; Fei, X.; Teng, Y.-B.; Rubin-Pitel, S.B.; Zhao, h.; Zhou C.-Z.
Crystal structure and computational analyses provide insights into the catalytic mechanism of 2,4-diacetylphloroglucinol hydrolase PhlG from Pseudomonas fluorescens
J. Biol. Chem.
285
4603-4611
2010
Pseudomonas fluorescens (Q4K423), Pseudomonas fluorescens, Pseudomonas fluorescens Pf-5 (Q4K423)
brenda
Ortet, P.; Barakat, M.; Lalaouna,D.; Fochesato, S.; Barbe, V.; Vacherie, B.; Santaella, C.; Heulin, T.; Achouak, W.
Complete genome sequence of a beneficial plant root-associated bacterium, Pseudomonas brassicacearum
J. Bacteriol.
193
3146
2011
Pseudomonas brassicacearum (F2KGR4), Pseudomonas brassicacearum NFM421 (F2KGR4)
brenda
Frank, A.; Siirola, E.; Kroutil, W.; Grogan, G.
Mutational analysis of the C-C bond cleaving enzyme phloretin hydrolase from Eubacterium ramulus
Topics Catal.
57
376-384
2014
Pseudomonas fluorescens (Q4K423)
-
brenda
Yan, X.; Yang, R.; Zhao, R.X.; Han, J.T.; Jia, W.J.; Li, D.Y.; Wang, Y.; Zhang, N.; Wu, Y.; Zhang, L.Q.; He, Y.X.
Transcriptional regulator PhlH modulates 2,4-diacetylphloroglucinol biosynthesis in response to the biosynthetic intermediate and end product
Appl. Environ. Microbiol.
83
e01419-17
2017
Pseudomonas fluorescens, Pseudomonas fluorescens (Q4JIX4), Pseudomonas fluorescens 2P24, Pseudomonas fluorescens 2P24 (Q4JIX4)
brenda
Someya, N.; Tsuchiya, K.; Yoshida, T.; Noguchi, M.; Akutsu, K.; Sawada, H.
Co-inoculation of an antibiotic-producing bacterium and a lytic enzyme-producing bacterium for the biocontrol of tomato wilt caused by Fusarium oxysporum f. sp. lycopersici
Biocontrol. Sci.
12
1-6
2007
Pseudomonas fluorescens, Pseudomonas fluorescens LRB3W1
brenda
Tian, T.; Sun, B.; Zhang, W.; Wei, J.; Li, W.; Zhang, L.
OmpR regulates the intracellular concentration of 2,4-diacetylphloroglucinol by affecting the transcriptional activity of the hydrolase phlG in Pseudomonas fluorescens 2P24
J. Pure Appl. Microbiol.
9
189-200
2015
Pseudomonas fluorescens, Pseudomonas fluorescens (Q4JIX4), Pseudomonas fluorescens 2P24, Pseudomonas fluorescens 2P24 (Q4JIX4)
-
brenda
Frank, A.; Siirola, E.; Kroutil, W.; Grogan, G.
Mutational analysis of the C-C bond cleaving enzyme phloretin hydrolase from Eubacterium ramulus
Top. Catal.
57
376-384
2014
Pseudomonas fluorescens (Q4K423), Pseudomonas fluorescens ATCC BAA-477 (Q4K423)
-
brenda
Mandryk-Litvinkovich, M.; Muratova, A.; Nosonova, T.; Evdokimova, O.; Valentovich, L.; Titok, M.; Kolomiets, E.
Molecular genetic analysis of determinants defining synthesis of 2,4-diacetylphloroglucinol by Pseudomonas brassicacearum BIM B-446 bacteria
Appl. Biochem. Microbiol.
53
31-39
2017
Pseudomonas brassicacearum (A0A125SE96), Pseudomonas brassicacearum BIM B-446 (A0A125SE96)
-
brenda