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IUBMB CommentsThis mycobacterial polyketide enzyme produces the hepta- and octa-methylated fatty acids known as phthioceranic acids, and presumably their hydroxylated versions. Formation of hepta- and octamethylated products depends on whether the enzyme incorporates seven or eight methylmalonyl-CoA extender units, respectively. Formation of hydroxylated products may result from the enzyme skipping the dehydratase (DH) and enoylreductase (ER) domains during the first cycle of condensation .
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(S)-methylmalonyl-CoA:palmitoyl-[(hydroxy)phthioceranic acid synthase] methylmalonyltransferase (phthioceranyl-[(hydroxy)phthioceranic acid synthase]-forming)
This mycobacterial polyketide enzyme produces the hepta- and octa-methylated fatty acids known as phthioceranic acids, and presumably their hydroxylated versions. Formation of hepta- and octamethylated products depends on whether the enzyme incorporates seven or eight methylmalonyl-CoA extender units, respectively. Formation of hydroxylated products may result from the enzyme skipping the dehydratase (DH) and enoylreductase (ER) domains during the first cycle of condensation [2].
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malfunction

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a pks2 gene disruption mutant is incapable of producing hepta- and octamethyl phthioceranic acids and hydroxyphthioceranic acids that are the major acyl constituents of sulfolipids. Consequently, the pks2 mutant does not produce sulfolipids
malfunction
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strains with a disruption of the pks2 gene do not synthesize sulfolipids
malfunction
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strains with a disruption of the pks2 gene do not synthesize sulfolipids
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malfunction
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a pks2 gene disruption mutant is incapable of producing hepta- and octamethyl phthioceranic acids and hydroxyphthioceranic acids that are the major acyl constituents of sulfolipids. Consequently, the pks2 mutant does not produce sulfolipids
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metabolism

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the enzyme is required for sulfolipid biosynthesis and synthesizes phthioceronic acids and hydroxyphthioceronic acids as the major components of mycobacterial sulfolipids
metabolism
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the enzyme synthesizes the methyl-branched fatty acyl components of sulfolipid-I
metabolism
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the enzyme synthesizes the methyl-branched fatty acyl components of sulfolipid-I
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Passemar, C.; Arbués, A.; Malaga, W.; Mercier, I.; Moreau, F.; Lepourry, L.; Neyrolles, O.; Guilhot, C.; Astarie-Dequeker, C.
Multiple deletions in the polyketide synthase gene repertoire of Mycobacterium tuberculosis reveal functional overlap of cell envelope lipids in host-pathogen interactions
Cell. Microbiol.
16
195-213
2014
Mycobacterium tuberculosis, Mycobacterium tuberculosis H37Rv
-
brenda
Sirakova, T.D.; Thirumala, A.K.; Dubey, V.S.; Sprecher, H.; Kolattukudy, P.E.
The Mycobacterium tuberculosis pks2 gene encodes the synthase for the hepta- and octamethyl-branched fatty acids required for sulfolipid synthesis
J. Biol. Chem.
276
16833-16839
2001
Mycobacterium tuberculosis, Mycobacterium tuberculosis H37Rv
brenda
Goyal, R.; Das, A.; Singh, R.; Singh, P.; Korpole, S.; Sarkar, D.
Phosphorylation of PhoP protein plays direct regulatory role in lipid biosynthesis of Mycobacterium tuberculosis
J. Biol. Chem.
286
45197-45208
2011
Mycobacterium tuberculosis, Mycobacterium tuberculosis H37Rv
-
brenda
Bhatt, K.; Gurcha, S.S.; Bhatt, A.; Besra, G.S.; Jacobs, W.R.
Two polyketide-synthase-associated acyltransferases are required for sulfolipid biosynthesis in Mycobacterium tuberculosis
Microbiology
153
513-520
2007
Mycobacterium tuberculosis, Mycobacterium tuberculosis H37Rv
brenda
Gokhale, R.; Saxena, P.; Chopra, T.; Mohanty, D.
Versatile polyketide enzymatic machinery for the biosynthesis of complex mycobacterial lipids
Nat. Prod. Rep.
24
267-277
2007
Mycobacterium tuberculosis
brenda
Zheng, D.; Schroeder, G.; Schroeder, J.; Hrazdina, G.
Molecular and biochemical characterization of three aromatic polyketide synthase genes from Rubus idaeus
Plant Mol. Biol.
46
1-15
2001
no activity in Rubus idaeus cultivar Royalty
brenda