2.3.1.261: (4-hydroxyphenyl)alkanoate synthase
This is an abbreviated version!
For detailed information about (4-hydroxyphenyl)alkanoate synthase, go to the full flat file.
Word Map on EC 2.3.1.261
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2.3.1.261
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polyketide
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ketosynthase
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at-less
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spoligotyping
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trans-at
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ketoreductase
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phenolphthiocerol
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phthiocerol
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leinamycin
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diagnostics
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euro-american
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indo-oceanic
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dimycocerosate
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nrps-pk
- 2.3.1.261
- polyketide
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ketosynthase
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at-less
-
spoligotyping
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trans-at
- ketoreductase
- phenolphthiocerol
- phthiocerol
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leinamycin
- diagnostics
-
euro-american
-
indo-oceanic
-
dimycocerosate
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nrps-pk
Reaction
+ 8 malonyl-CoA + 16 NADPH + 16 H+ = + 8 CO2 + 8 CoA + 16 NADP+ + 8 H2O
Synonyms
4-hydroxyphenylalkanoate synthase, msl7, PKS1, Pks15, Pks15/1, type I PKS
ECTree
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General Information
General Information on EC 2.3.1.261 - (4-hydroxyphenyl)alkanoate synthase
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malfunction
physiological function
the Dpks15 mutant has a slight reduction in radial growth and produces fewer spores compared to wild-type. Insect bioassays indicate the DELTApks15 mutant to be significantly reduced in virulence against beet armyworms compared to wild-type, which can be partially accounted for by its markedly decreased ability to survive phagocytosis. Total haemocyte count decreases sharply by 50fold from days 1-3 post-inoculation in insects infected with wild-type, compared to a 5fold decrease in the DELTApks15 mutant. The mutant also produces 3fold fewer hemolymph hyphal bodies than the wild-type. In co-culture studies with amoebae that have phagocytic ability similar to that of insect haemocytes, the mortality rate of amoebae engulfing DELTApks15 decreases by 72% during 48 h, and DELTApks15 CFU decrease by 83% compared to co-culture with the wild-type. Thus, the DELTApks15 mutant has a reduced ability to cope with phagocytosis and highly reduced virulence in an insect host
malfunction
Beauveria bassiana BCC2660
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the Dpks15 mutant has a slight reduction in radial growth and produces fewer spores compared to wild-type. Insect bioassays indicate the DELTApks15 mutant to be significantly reduced in virulence against beet armyworms compared to wild-type, which can be partially accounted for by its markedly decreased ability to survive phagocytosis. Total haemocyte count decreases sharply by 50fold from days 1-3 post-inoculation in insects infected with wild-type, compared to a 5fold decrease in the DELTApks15 mutant. The mutant also produces 3fold fewer hemolymph hyphal bodies than the wild-type. In co-culture studies with amoebae that have phagocytic ability similar to that of insect haemocytes, the mortality rate of amoebae engulfing DELTApks15 decreases by 72% during 48 h, and DELTApks15 CFU decrease by 83% compared to co-culture with the wild-type. Thus, the DELTApks15 mutant has a reduced ability to cope with phagocytosis and highly reduced virulence in an insect host
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4-hydroxybenzoic acid-AMP ligase FadD22 catalyzes the activation of 4-hydroxybenzoic acid and its subsequent transfer onto PKS15/1, to yield 4-hydroxyphenylalkanoate. This latter lipid is then activated by 4-hydroxyphenylalkanoate adenylyltransferase FadD29 and transferred onto PpsA. Overview on biosynthesis of phthiocerol and phthiodiolone dimycocerosates
physiological function
a gene disruption mutant is not able to produce dimycocerosyl phthiocerol, although it can produce mycocerosic acids. The mutant is attenuated in a murine model, supporting the hypothesis that dimycocerosyl phthiocerol is a virulence factor
physiological function
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a single open reading frame for pks15/1 is found in Mycobacterium bovis BCG. Disruption of the pks15/1 gene leads to the abolition of the synthesis of type-specific phenolphthiocerol glycolipid
physiological function
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comparison of amino acid sequence homology relationships among the mas-like (msl) genes and their domain organization in Mycobacterium tuberculosis
physiological function
polyketide synthase gene pks1 is involved in the elongation of 4hydroxybenzoic acid derivatives to form p-hydroxyphenylalkanoates, which in turn are converted, presumably by the PpsA-E synthase, to phenolphthiocerol derivatives. All the strains of Mycobacterium tuberculosis examined and deficient in the production of phenolphthiocerol derivatives are natural mutants with a frameshift mutation in pks1
physiological function
polyketide synthase gene pks15 is involved in the elongation of 4-hydroxybenzoic acid derivatives to form p-hydroxyphenylalkanoates, which in turn are converted, presumably by the PpsA-E synthase, to phenolphthiocerol derivatives. All the strains of Mycobacterium tuberculosis examined and deficient in the production of phenolphthiocerol derivatives are natural mutants with a frameshift mutation in pks15
physiological function
the pks15/1 gene is a virulence marker in Mycobacterium tuberculosis
physiological function
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4-hydroxybenzoic acid-AMP ligase FadD22 catalyzes the activation of 4-hydroxybenzoic acid and its subsequent transfer onto PKS15/1, to yield 4-hydroxyphenylalkanoate. This latter lipid is then activated by 4-hydroxyphenylalkanoate adenylyltransferase FadD29 and transferred onto PpsA. Overview on biosynthesis of phthiocerol and phthiodiolone dimycocerosates
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physiological function
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the pks15/1 gene is a virulence marker in Mycobacterium tuberculosis
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physiological function
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a gene disruption mutant is not able to produce dimycocerosyl phthiocerol, although it can produce mycocerosic acids. The mutant is attenuated in a murine model, supporting the hypothesis that dimycocerosyl phthiocerol is a virulence factor
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