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IUBMB CommentsThe enzyme, present in pathogenic species of mycobacteria, participates in the pathway for biosynthesis of phthiocerols. It catalyses the adenylation of the long-chain fatty acids arachidate (C20) or behenate (C22) and potentially the very-long-chain fatty acid lignocerate (C24) . The activated fatty acids are then loaded to EC 2.3.1.292, (phenol)carboxyphthiodiolenone synthase.
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a long-chain fatty-acyl adenylate ester + holo-[(phenol)carboxyphthiodiolenone synthase]
AMP + a long-chain acyl-[(phenol)carboxyphthiodiolenone synthase]
ATP + a long-chain fatty acid
diphosphate + a long-chain fatty-acyl adenylate ester
ATP + a long-chain fatty acid + holo-[(phenol)carboxyphthiodiolenone synthase]
AMP + diphosphate + a long-chain acyl-[(phenol)carboxyphthiodiolenone synthase]
additional information
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a long-chain fatty-acyl adenylate ester + holo-[(phenol)carboxyphthiodiolenone synthase]
AMP + a long-chain acyl-[(phenol)carboxyphthiodiolenone synthase]
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a long-chain fatty-acyl adenylate ester + holo-[(phenol)carboxyphthiodiolenone synthase]
AMP + a long-chain acyl-[(phenol)carboxyphthiodiolenone synthase]
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a long-chain fatty-acyl adenylate ester + holo-[(phenol)carboxyphthiodiolenone synthase]
AMP + a long-chain acyl-[(phenol)carboxyphthiodiolenone synthase]
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ATP + a long-chain fatty acid
diphosphate + a long-chain fatty-acyl adenylate ester
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ATP + a long-chain fatty acid
diphosphate + a long-chain fatty-acyl adenylate ester
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ATP + a long-chain fatty acid
diphosphate + a long-chain fatty-acyl adenylate ester
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ATP + a long-chain fatty acid + holo-[(phenol)carboxyphthiodiolenone synthase]
AMP + diphosphate + a long-chain acyl-[(phenol)carboxyphthiodiolenone synthase]
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ATP + a long-chain fatty acid + holo-[(phenol)carboxyphthiodiolenone synthase]
AMP + diphosphate + a long-chain acyl-[(phenol)carboxyphthiodiolenone synthase]
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ATP + a long-chain fatty acid + holo-[(phenol)carboxyphthiodiolenone synthase]
AMP + diphosphate + a long-chain acyl-[(phenol)carboxyphthiodiolenone synthase]
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additional information
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in vivo, FadD26 specificallyactivates C22-24 fatty acyl chains that are loaded onto phenolcarboxyphthiodiolenone synthase PpsA for the formation of the phthiocerol chain, but FadD26 is not required for the production of phenolic glycolipids
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additional information
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in vivo, FadD26 specifically activates C22-24 fatty acyl chains that are loaded onto phenolcarboxyphthiodiolenone synthase PpsA for the formation of the phthiocerol chain, but FadD26 is not required for the production of phenolic glycolipids
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a long-chain fatty-acyl adenylate ester + holo-[(phenol)carboxyphthiodiolenone synthase]
AMP + a long-chain acyl-[(phenol)carboxyphthiodiolenone synthase]
-
-
-
?
ATP + a long-chain fatty acid
diphosphate + a long-chain fatty-acyl adenylate ester
-
-
-
?
ATP + a long-chain fatty acid + holo-[(phenol)carboxyphthiodiolenone synthase]
AMP + diphosphate + a long-chain acyl-[(phenol)carboxyphthiodiolenone synthase]
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?
additional information
?
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in vivo, FadD26 specificallyactivates C22-24 fatty acyl chains that are loaded onto phenolcarboxyphthiodiolenone synthase PpsA for the formation of the phthiocerol chain, but FadD26 is not required for the production of phenolic glycolipids
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Infections
T-cell responses and in vivo cytotoxicity in the target organ and the regional lymphoid tissue during airborne infection with the virulent Mycobacterium tuberculosis MT103 and its lipid mutant fadD26.
long-chain fatty acid adenylase/transferase fadd26 deficiency
Effect of phthiocerol dimycocerosate deficiency on the transcriptional response of human macrophages to Mycobacterium tuberculosis.
Pneumonia
Immunogenicity and protective efficacy of the Mycobacterium tuberculosis fadD26 mutant.
Tuberculosis
Analysis of the phthiocerol dimycocerosate locus of Mycobacterium tuberculosis. Evidence that this lipid is involved in the cell wall permeability barrier.
Tuberculosis
Comparative Metabolomics between Mycobacterium tuberculosis and the MTBVAC Vaccine Candidate.
Tuberculosis
Construction and Characterization of the Mycobacterium tuberculosis sigE fadD26 Unmarked Double Mutant as a Vaccine Candidate.
Tuberculosis
Construction, characterization and preclinical evaluation of MTBVAC, the first live-attenuated M. tuberculosis-based vaccine to enter clinical trials.
Tuberculosis
Delineation of the roles of FadD22, FadD26 and FadD29 in the biosynthesis of phthiocerol dimycocerosates and related compounds in Mycobacterium tuberculosis.
Tuberculosis
Effect of phthiocerol dimycocerosate deficiency on the transcriptional response of human macrophages to Mycobacterium tuberculosis.
Tuberculosis
Hyper-attenuated MTBVAC erp mutant protects against tuberculosis in mice.
Tuberculosis
Immunogenicity and protective efficacy of the Mycobacterium tuberculosis fadD26 mutant.
Tuberculosis
T-cell responses and in vivo cytotoxicity in the target organ and the regional lymphoid tissue during airborne infection with the virulent Mycobacterium tuberculosis MT103 and its lipid mutant fadD26.
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physiological function
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a FadD26 mutant has impaired synthesis of phthiocerol dimycocerosates and is attenuated in BALB/c mice. The FadD26 mutant induces less pneumonia and larger delayed-type hypersensitivity reactions. It induces lower but progressive production of interferon-gamma, interleukin-4 and tumour necrosis factor-alpha. Used as a subcutaneous vaccine, the mutant induces a higher level of protection than does strain Bacille Calmette-Guérin (BCG). There is less tissue damage (pneumonia) and lower colony-forming units in the mice vaccinated with the FadD26 mutant compared to the findings in mice vaccinated with BCG
physiological function
FadD26 is required for the production of phthiodiolone dimycocerosates but not of phenolic glycolipids. Disruption of FadD26 in Mycobacterium bovis BCG abolishes the production of phthiocerol dimycocerosate (DIM A) and of phthiodiolone dimycocerosate (DIM B)
physiological function
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mutants lacking the Pps1-5 gene cluster are not able to produce phenolphthiocerol derivative, mycoside B, or phthiocerol dimycocerosates
physiological function
PpsA, the first-acting enzyme of a multisubunit noniterative polyketide synthase system is loaded with fatty acids by specific fatty acyl-AMP ligase FadD26 for biosynthesis of phthiocerol dimycocerosates. Deletion of fadD26 produces selective loss of phthiocerol dimycocerosates
physiological function
-
a FadD26 mutant has impaired synthesis of phthiocerol dimycocerosates and is attenuated in BALB/c mice. The FadD26 mutant induces less pneumonia and larger delayed-type hypersensitivity reactions. It induces lower but progressive production of interferon-gamma, interleukin-4 and tumour necrosis factor-alpha. Used as a subcutaneous vaccine, the mutant induces a higher level of protection than does strain Bacille Calmette-Guérin (BCG). There is less tissue damage (pneumonia) and lower colony-forming units in the mice vaccinated with the FadD26 mutant compared to the findings in mice vaccinated with BCG
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physiological function
-
PpsA, the first-acting enzyme of a multisubunit noniterative polyketide synthase system is loaded with fatty acids by specific fatty acyl-AMP ligase FadD26 for biosynthesis of phthiocerol dimycocerosates. Deletion of fadD26 produces selective loss of phthiocerol dimycocerosates
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medicine
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a FadD26 mutant has impaired synthesis of phthiocerol dimycocerosates and is attenuated in BALB/c mice. The FadD26 mutant induces less pneumonia and larger delayed-type hypersensitivity reactions. It induces lower but progressive production of interferon-gamma, interleukin-4 and tumour necrosis factor-alpha. Used as a subcutaneous vaccine, the mutant induces a higher level of protection than does strain Bacille Calmette-Guérin (BCG). There is less tissue damage (pneumonia) and lower colony-forming units in the mice vaccinated with the FadD26 mutant compared to the findings in mice vaccinated with BCG
medicine
a SigE/FadD26 double mutant is more attenuated and more efficacious than wild-type strain BCG BCG in a mouse model of infection, and equivalent to BCG in a Guinea pig model of infection
medicine
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comparison of parental virulent clinical isolate MT103 with its mutant FadD26, lacking phthiocerol dimycocerosates. Upon airways infection both mycobacteria behave similarly regarding T cell stimulation kinetics. They differ in the magnitude of these responses, in the bacterial load within tissues, and to trigger in vivo cytotoxicity in lungs and regional lymph nodes
medicine
-
a FadD26 mutant has impaired synthesis of phthiocerol dimycocerosates and is attenuated in BALB/c mice. The FadD26 mutant induces less pneumonia and larger delayed-type hypersensitivity reactions. It induces lower but progressive production of interferon-gamma, interleukin-4 and tumour necrosis factor-alpha. Used as a subcutaneous vaccine, the mutant induces a higher level of protection than does strain Bacille Calmette-Guérin (BCG). There is less tissue damage (pneumonia) and lower colony-forming units in the mice vaccinated with the FadD26 mutant compared to the findings in mice vaccinated with BCG
-
medicine
-
comparison of parental virulent clinical isolate MT103 with its mutant FadD26, lacking phthiocerol dimycocerosates. Upon airways infection both mycobacteria behave similarly regarding T cell stimulation kinetics. They differ in the magnitude of these responses, in the bacterial load within tissues, and to trigger in vivo cytotoxicity in lungs and regional lymph nodes
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Simeone, R; Lger, M.; Constant, P.; Malaga, W.; Marrakchi, H.; Daff, M.; Guilhot, C.; Chalut, C.
Delineation of the roles of FadD22, FadD26 and FadD29 in the biosynthesis of phthiocerol dimycocerosates and related compounds in Mycobacterium tuberculosis
FEBS J.
277
2715-2725
2010
Mycobacterium tuberculosis variant bovis (A0A0H3M8A6)
brenda
Vergnolle, O.; Chavadi, S.S.; Edupuganti, U.R.; Mohandas, P.; Chan, C.; Zeng, J.; Kopylov, M.; Angelo, N.G.; Warren, J.D.; Soll, C.E.; Quadri, L.E.
Biosynthesis of cell envelope-associated phenolic glycolipids in Mycobacterium marinum
J. Bacteriol.
197
1040-1050
2015
Mycobacterium marinum (B2HIN2), Mycobacterium marinum BAA-535 (B2HIN2)
brenda
Infante, E.; Aguilar, L.D.; Gicquel, B.; Pando, R.H.
Immunogenicity and protective efficacy of the Mycobacterium tuberculosis fadD26 mutant
Clin. Exp. Immunol.
141
21-28
2005
Mycobacterium tuberculosis, Mycobacterium tuberculosis MT103
brenda
Hernandez Pando, R.; Shin, S.J.; Clark, S.; Casonato, S.; Zambrano, M.B.; Kim, H.; Boldrin, F.; Mata Espinoza, D.; Provvedi, R.; Arbues, A.; Marquina Castillo, B.; Cioetto Mazzabo, L.; Barrios Payan, J.; Martin, C.; Cho, S.N.; Williams, A.; Manganelli, R.
Construction and characterization of the double unmarked Mycobacterium tuberculosis mutant sigE/fadD26 as a vaccine candidate
Infect. Immun.
88
e00496
2019
Mycobacterium tuberculosis variant bovis (A0A0H3M8A6)
brenda
Azad, A.; Sirakova, T.; Fernandes, N.; Kolattukudy, P.
Gene knockout reveals a novel gene cluster for the synthesis of a class of cell wall lipids unique to pathogenic mycobacteria
J. Biol. Chem.
272
16741-16745
1997
Mycobacterium tuberculosis variant bovis
brenda
Quintero-Macias, L.; Santos-Mendoza, T.; Donis-Maturano, L.; Silva-Sanchez, A.; Aguilar, D.; Orozco, H.; Gicquel, B.; Estrada-Garcia, I.; Flores-Romo, L.; Hernandez-Pando, R.
T-cell responses and in vivo cytotoxicity in the target organ and the regional lymphoid tissue during airborne infection with the virulent Mycobacterium tuberculosis MT103 and its lipid mutant fadD26
Scand. J. Immunol.
71
20-28
2010
Mycobacterium tuberculosis, Mycobacterium tuberculosis MT103
brenda
6.2.1.59 long-chain fatty acid adenylase/transferase FadD26
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