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Information on EC 2.3.1.282 - phenolphthiocerol/phthiocerol/phthiodiolone dimycocerosyl transferase
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2.3.1.282 phenolphthiocerol/phthiocerol/phthiodiolone dimycocerosyl transferaseIUBMB Comments
The enzyme, present in certain pathogenic species of mycobacteria, catalyses the transfer of mycocerosic acids to the two hydroxyl groups at the common lipid core of phthiocerol, phthiodiolone, and phenolphthiocerol, forming dimycocerosate esters. The fatty acid precursors of mycocerosic acids are activated by EC 6.2.1.49, long-chain fatty acid adenylyltransferase FadD28, which loads them onto EC 2.3.1.111, mycocerosate synthase. That enzyme extends the precursors to form mycocerosic acids that remain attached until transferred by EC 2.3.1.282.
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Word Map
- 2.3.1.282
- tuberculosis
- acyltransferase
-
dimycocerosate
-
pdims
- esterification
-
fadd28
- chloramphenicol
-
virulence-enhancing
- rifamycin
-
two-domain
- transacetylase
- carnitine
-
dihydrolipoyl
- synthesis
The enzyme appears in viruses and cellular organisms
Reaction Schemes
2
+
=
+
2
2
a mycocerosyl-[mycocerosic acid synthase]
+
a phthiocerol
=
a dimycocerosyl phthiocerol
+
2
holo-[mycocerosic acid synthase]
2
+
=
+
2
2
a mycocerosyl-[mycocerosic acid synthase]
+
a phthiodiolone
=
a dimycocerosyl phthiodiolone
+
2
holo-[mycocerosic acid synthase]
2
+
=
+
2
2
a mycocerosyl-[mycocerosic acid synthase]
+
a phenolphthiocerol
=
a dimycocerosyl phenolphthiocerol
+
2
holo-[mycocerosic acid synthase]
Synonyms
papa5, polyketide-associated protein a5, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
papA5
polyketide-associated protein A5
papA5
-
-
-
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
2 a mycocerosyl-[mycocerosic acid synthase] + a phenolphthiocerol = a dimycocerosyl phenolphthiocerol + 2 holo-[mycocerosic acid synthase]
(3)
-
-
-
2 a mycocerosyl-[mycocerosic acid synthase] + a phthiocerol = a dimycocerosyl phthiocerol + 2 holo-[mycocerosic acid synthase]
(1)
-
-
-
2 a mycocerosyl-[mycocerosic acid synthase] + a phthiodiolone = a dimycocerosyl phthiodiolone + 2 holo-[mycocerosic acid synthase]
(2)
-
-
-
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PATHWAY SOURCE
PATHWAYS
-
,
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SYSTEMATIC NAME
IUBMB Comments
mycocerosyl-[mycocerosic acid synthase]:phenolphthiocerol/phthiocerol/phthiodiolone dimycocerosyl transferase
The enzyme, present in certain pathogenic species of mycobacteria, catalyses the transfer of mycocerosic acids to the two hydroxyl groups at the common lipid core of phthiocerol, phthiodiolone, and phenolphthiocerol, forming dimycocerosate esters. The fatty acid precursors of mycocerosic acids are activated by EC 6.2.1.49, long-chain fatty acid adenylyltransferase FadD28, which loads them onto EC 2.3.1.111, mycocerosate synthase. That enzyme extends the precursors to form mycocerosic acids that remain attached until transferred by EC 2.3.1.282.
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
2 a mycocerosyl-[mycocerosic acid synthase] + a phenolphthiocerol
a dimycocerosyl phenolphthiocerol + 2 holo-[mycocerosic acid synthase]
2 a mycocerosyl-[mycocerosic acid synthase] + a phthiocerol
a dimycocerosyl phthiocerol + 2 holo-[mycocerosic acid synthase]
2 a mycocerosyl-[mycocerosic acid synthase] + a phthiodiolone
a dimycocerosyl phthiodiolone + 2 holo-[mycocerosic acid synthase]
2 palmitoyl-CoA + 5R,7R-pentadecane-5,7-diol
5,7-dipalmitoyl 5R,7R-pentadecane-5,7-diol + 2 CoA
2 palmitoyl-CoA + glycosyl-phenolphthiocerol
dipalmitoyl glycosyl-phenolphthiocerol + 2 CoA
lauroyl-[mycocerosic acid synthase] + 2-dodecanol
2-dodecanyl dodecanoate + holo-[mycocerosic acid synthase]
octan-1-ol + heptadecanoyl-CoA
1-octyl heptadecanoate + CoA
-
-
-
?
(R)-octan-2-ol + palmitoyl-CoA
(R)-2-octanyl palmitate + CoA
-
-
-
?
(R)-octan-2-ol + palmitoyl-CoA
(R)-2-octanyl palmitate + CoA
-
-
-
?
(R,S)-octan-2-ol + palmitoyl-CoA
(R,S)-2-octanyl palmitate + CoA
-
-
-
?
(R,S)-octan-2-ol + palmitoyl-CoA
(R,S)-2-octanyl palmitate + CoA
-
-
-
?
2 a mycocerosyl-[mycocerosic acid synthase] + a phenolphthiocerol
a dimycocerosyl phenolphthiocerol + 2 holo-[mycocerosic acid synthase]
-
-
-
?
2 a mycocerosyl-[mycocerosic acid synthase] + a phenolphthiocerol
a dimycocerosyl phenolphthiocerol + 2 holo-[mycocerosic acid synthase]
-
-
-
?
2 a mycocerosyl-[mycocerosic acid synthase] + a phthiocerol
a dimycocerosyl phthiocerol + 2 holo-[mycocerosic acid synthase]
-
-
-
?
2 a mycocerosyl-[mycocerosic acid synthase] + a phthiocerol
a dimycocerosyl phthiocerol + 2 holo-[mycocerosic acid synthase]
-
-
-
?
2 a mycocerosyl-[mycocerosic acid synthase] + a phthiodiolone
a dimycocerosyl phthiodiolone + 2 holo-[mycocerosic acid synthase]
-
-
-
?
2 a mycocerosyl-[mycocerosic acid synthase] + a phthiodiolone
a dimycocerosyl phthiodiolone + 2 holo-[mycocerosic acid synthase]
-
-
-
?
2 palmitoyl-CoA + 5R,7R-pentadecane-5,7-diol
5,7-dipalmitoyl 5R,7R-pentadecane-5,7-diol + 2 CoA
-
-
-
?
2 palmitoyl-CoA + 5R,7R-pentadecane-5,7-diol
5,7-dipalmitoyl 5R,7R-pentadecane-5,7-diol + 2 CoA
-
-
-
?
2 palmitoyl-CoA + 5R,7R-undecane-5,7-diol
5,7-dipalmitoyl 5R,7R-undecane-5,7-diol + 2 CoA
-
-
-
?
2 palmitoyl-CoA + 5R,7R-undecane-5,7-diol
5,7-dipalmitoyl 5R,7R-undecane-5,7-diol + 2 CoA
-
-
-
?
2 palmitoyl-CoA + glycosyl-phenolphthiocerol
dipalmitoyl glycosyl-phenolphthiocerol + 2 CoA
substrate isolated from Mycobacterium leprae in infected Armadillo tissue
-
-
?
2 palmitoyl-CoA + glycosyl-phenolphthiocerol
dipalmitoyl glycosyl-phenolphthiocerol + 2 CoA
substrate isolated from Mycobacterium leprae in infected Armadillo tissue
-
-
?
decan-1-ol + palmitoyl-CoA
1-decyl palmitate + CoA
-
-
-
?
hexadecanol + palmitoyl-CoA
hexadecyl palmitate + CoA
-
-
-
?
hexadecanol + palmitoyl-CoA
hexadecyl palmitate + CoA
-
-
-
?
lauroyl-[mycocerosic acid synthase] + 2-dodecanol
2-dodecanyl dodecanoate + holo-[mycocerosic acid synthase]
-
-
-
?
lauroyl-[mycocerosic acid synthase] + 2-dodecanol
2-dodecanyl dodecanoate + holo-[mycocerosic acid synthase]
-
-
-
?
palmitoyl-CoA + 1-octanol
palmitoyl octanol + 2 CoA
-
-
-
?
palmitoyl-CoA + 1-octanol
palmitoyl octanol + 2 CoA
-
-
-
?
additional information
?
-
PapA5 protein directly transfers the protein bound mycocerosic acid analogs on phthiocerol to catalyze the final esterification step of phthiocerol dimycocerisate
-
-
?
additional information
?
-
-
PapA5 protein directly transfers the protein bound mycocerosic acid analogs on phthiocerol to catalyze the final esterification step of phthiocerol dimycocerisate
-
-
?
additional information
?
-
enzyme shows a preference for saturated medium chain alcohols, with 1-octanol displaying the highest ester formation stoichiometry. 20- and 5fold more ester is formed with (R)-(-)2-octanol and (S)-(-)1,2-decanediol, respectively, than with their corresponding enantiomers
-
-
?
additional information
?
-
-
enzyme shows a preference for saturated medium chain alcohols, with 1-octanol displaying the highest ester formation stoichiometry. 20- and 5fold more ester is formed with (R)-(-)2-octanol and (S)-(-)1,2-decanediol, respectively, than with their corresponding enantiomers
-
-
?
additional information
?
-
enzyme shows a preference for saturated medium chain alcohols, with 1-octanol displaying the highest ester formation stoichiometry. 20- and 5fold more ester is formed with (R)-(-)2-octanol and (S)-(-)1,2-decanediol, respectively, than with their corresponding enantiomers
-
-
?
additional information
?
-
PapA5 protein directly transfers the protein bound mycocerosic acid analogs on phthiocerol to catalyze the final esterification step of phthiocerol dimycocerisate
-
-
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
2 a mycocerosyl-[mycocerosic acid synthase] + a phenolphthiocerol
a dimycocerosyl phenolphthiocerol + 2 holo-[mycocerosic acid synthase]
2 a mycocerosyl-[mycocerosic acid synthase] + a phthiocerol
a dimycocerosyl phthiocerol + 2 holo-[mycocerosic acid synthase]
2 a mycocerosyl-[mycocerosic acid synthase] + a phthiodiolone
a dimycocerosyl phthiodiolone + 2 holo-[mycocerosic acid synthase]
2 a mycocerosyl-[mycocerosic acid synthase] + a phenolphthiocerol
a dimycocerosyl phenolphthiocerol + 2 holo-[mycocerosic acid synthase]
-
-
-
?
2 a mycocerosyl-[mycocerosic acid synthase] + a phenolphthiocerol
a dimycocerosyl phenolphthiocerol + 2 holo-[mycocerosic acid synthase]
-
-
-
?
2 a mycocerosyl-[mycocerosic acid synthase] + a phthiocerol
a dimycocerosyl phthiocerol + 2 holo-[mycocerosic acid synthase]
-
-
-
?
2 a mycocerosyl-[mycocerosic acid synthase] + a phthiocerol
a dimycocerosyl phthiocerol + 2 holo-[mycocerosic acid synthase]
-
-
-
?
2 a mycocerosyl-[mycocerosic acid synthase] + a phthiodiolone
a dimycocerosyl phthiodiolone + 2 holo-[mycocerosic acid synthase]
-
-
-
?
2 a mycocerosyl-[mycocerosic acid synthase] + a phthiodiolone
a dimycocerosyl phthiodiolone + 2 holo-[mycocerosic acid synthase]
-
-
-
?
additional information
?
-
PapA5 protein directly transfers the protein bound mycocerosic acid analogs on phthiocerol to catalyze the final esterification step of phthiocerol dimycocerisate
-
-
?
additional information
?
-
-
PapA5 protein directly transfers the protein bound mycocerosic acid analogs on phthiocerol to catalyze the final esterification step of phthiocerol dimycocerisate
-
-
?
additional information
?
-
PapA5 protein directly transfers the protein bound mycocerosic acid analogs on phthiocerol to catalyze the final esterification step of phthiocerol dimycocerisate
-
-
?
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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DISEASE
TITLE OF PUBLICATION
LINK TO PUBMED
Tuberculosis
A homologue of the Mycobacterium tuberculosis PapA5 protein, rif-orf20, is an acetyltransferase involved in the biosynthesis of antitubercular drug rifamycin B by Amycolatopsis mediterranei S699.
Tuberculosis
Crystal structure of PapA5, a phthiocerol dimycocerosyl transferase from Mycobacterium tuberculosis.
Tuberculosis
Diacyltransferase Activity and Chain Length Specificity of Mycobacterium tuberculosis PapA5 in the Synthesis of Alkyl ?-Diol Lipids.
Tuberculosis
FHA domain containing protein Rv0019c and Polyketide-associated protein PapA5, from substrates of Serine/Threonine Protein Kinase PknB to interacting proteins of Mycobacterium tuberculosis.
Tuberculosis
Modification of PapA5 acyltransferase substrate selectivity for optimization of short-chain alcohol-derived multimethyl-branched ester production in Escherichia coli.
Tuberculosis
Mycobacterial polyketide-associated proteins are acyltransferases: proof of principle with Mycobacterium tuberculosis PapA5.
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
311
wild-type, substrate 5R,7R-undecane-5,7-diol, pH 6.5, 22°C
454
wild-type, substrate 5R,7R-pentadecane-5,7-diol, pH 6.5, 22°C
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
physiological function
physiological function
PapA5 catalyzes diesterification of phthiocerol and phthiodiolone with mycocerosate. Presence of PapA5 is required for synthesis of phthiocerol and phthiodiolone dimycocerosate esters
physiological function
Papa5 interacts with FHA domain-containing protein Rv0019c. The residues N-terminal to the functional FHA domain of Rv0019c are critical for formation of the Rv0019c-PapA5 complex
physiological function
PapA5 is essential for production of phenolic glycolipids. PapA5 catalyses the acylation of diol-containing polyketides to form of phenolic glycolipids
physiological function
PapA5 is the terminal enzyme in dimycocerosate biosynthesis with dual esterification activity
physiological function
-
PapA5 is essential for production of phenolic glycolipids. PapA5 catalyses the acylation of diol-containing polyketides to form of phenolic glycolipids
-
physiological function
-
PapA5 is the terminal enzyme in dimycocerosate biosynthesis with dual esterification activity
-
physiological function
-
Papa5 interacts with FHA domain-containing protein Rv0019c. The residues N-terminal to the functional FHA domain of Rv0019c are critical for formation of the Rv0019c-PapA5 complex
-
physiological function
-
PapA5 catalyzes diesterification of phthiocerol and phthiodiolone with mycocerosate. Presence of PapA5 is required for synthesis of phthiocerol and phthiodiolone dimycocerosate esters
-
Show AA Sequence and Transmembrane Helices (753 entries)
Please use the AA Sequence and Transmembrane Helices Search for a specific query.
Please use the AA Sequence and Transmembrane Helices Search for a specific query.
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POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
phosphoprotein
phosphoprotein
PapA5 is phosphorylated on threonine residues by kinase PknB, and serine/threonine phosphatase Mstp completely reverses the phosphorylation
phosphoprotein
Ser/Thr kinases PknB and PknE modify PapA5 on three overlapping Thr residues and a fourth Thr is unique to PknE phosphorylation
phosphoprotein
-
Ser/Thr kinases PknB and PknE modify PapA5 on three overlapping Thr residues and a fourth Thr is unique to PknE phosphorylation
-
phosphoprotein
-
PapA5 is phosphorylated on threonine residues by kinase PknB, and serine/threonine phosphatase Mstp completely reverses the phosphorylation
-
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
homology modeling and docking of modeled mycocerosic acid synthase docked on the structure of PapA5
to 2.75 A resoultion. The PapA5 active site includes conserved histidine and aspartic acid residues that are critical to PapA5 acyltransferase activity. Two hydrophobic channels link the PapA5 surface to the active. An additional alpha helix blocks the putative entrance into the PapA5 active site
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
A382M
35% of wild-type activity with substrate 1-octanol, 39% with 5R,7R-undecane-5,7-diol, 48% with pentadecane-5,7-diol, respectively
G129L
13% of wild-type activity with substrate 1-octanol, 4% with 5R,7R-undecane-5,7-diol, 13% with pentadecane-5,7-diol, respectively
Q19K
16% of wild-type activity with substrate 1-octanol, 11% with pentadecane-5,7-diol, respectively
Q19R
68% of wild-type activity with substrate 1-octanol, 48% with 5R,7R-undecane-5,7-diol, 45% with pentadecane-5,7-diol, respectively
V16C/G328C
8% of wild-type activity with with 5R,7R-undecane-5,7-diol, 3% with pentadecane-5,7-diol, respectively
A382M
-
35% of wild-type activity with substrate 1-octanol, 39% with 5R,7R-undecane-5,7-diol, 48% with pentadecane-5,7-diol, respectively
-
G129L
-
13% of wild-type activity with substrate 1-octanol, 4% with 5R,7R-undecane-5,7-diol, 13% with pentadecane-5,7-diol, respectively
-
Q19R
-
68% of wild-type activity with substrate 1-octanol, 48% with 5R,7R-undecane-5,7-diol, 45% with pentadecane-5,7-diol, respectively
-
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
synthesis
synthesis
use of PapA5 and a mutant mycocerosic acid synthase for synthesis of nonmethylated variants of mycocerosate esters
synthesis
-
use of PapA5 and a mutant mycocerosic acid synthase for synthesis of nonmethylated variants of mycocerosate esters
-
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Touchette, M.H.; Bommineni, G.R.; Delle Bovi, R.J.; Gadbery, J.E.; Nicora, C.D.; Shukla, A.K.; Kyle, J.E.; Metz, T.O.; Martin, D.W.; Sampson, N.S.; Miller, W.T.; Tonge, P.J.; Seeliger, J.C.
Diacyltransferase activity and chain length specificity of Mycobacterium tuberculosis PapA5 in the synthesis of alkyl beta-diol lipids
Biochemistry
54
5457-5468
2015
Mycobacterium tuberculosis (P9WIN5), Mycobacterium tuberculosis, Mycobacterium tuberculosis H37Rv (P9WIN5)
brenda
Buglino, J.; Onwueme, K.C.; Ferreras, J.A.; Quadri, L.E.; Lima, C.D.
Crystal structure of PapA5, a phthiocerol dimycocerosyl transferase from Mycobacterium tuberculosis
J. Biol. Chem.
279
30634-30642
2004
Mycobacterium tuberculosis (P9WIN5), Mycobacterium tuberculosis, Mycobacterium tuberculosis H37Rv (P9WIN5)
brenda
Gupta, M.; Sajid, A.; Arora, G.; Tandon, V.; Singh, Y.
Forkhead-associated domain-containing protein Rv0019c and polyketide-associated protein PapA5, from substrates of serine/threonine protein kinase PknB to interacting proteins of Mycobacterium tuberculosis
J. Biol. Chem.
284
34723-34734
2009
Mycobacterium tuberculosis (P9WIN5), Mycobacterium tuberculosis, Mycobacterium tuberculosis H37Rv (P9WIN5)
brenda
Chavadi, S.S.; Onwueme, K.C.; Edupuganti, U.R.; Jerome, J.; Chatterjee, D.; Soll, C.E.; Quadri, L.E.
The mycobacterial acyltransferase PapA5 is required for biosynthesis of cell wall-associated phenolic glycolipids
Microbiology
158
1379-1387
2012
Mycobacterium marinum (B2HIM3), Mycobacterium marinum ATCC BAA-535 (B2HIM3)
brenda
Trivedi, O.A.; Arora, P.; Vats, A.; Ansari, M.Z.; Tickoo, R.; Sridharan, V.; Mohanty, D.; Gokhale, R.S.
Dissecting the mechanism and assembly of a complex virulence mycobacterial lipid
Mol. Cell
17
631-643
2005
Mycobacterium tuberculosis (P9WIN5), Mycobacterium tuberculosis, Mycobacterium tuberculosis H37Rv (P9WIN5)
brenda
Onwueme, K.C.; Ferreras, J.A.; Buglino, J.; Lima, C.D.; Quadri, L.E.
Mycobacterial polyketide-associated proteins are acyltransferases proof of principle with Mycobacterium tuberculosis PapA5
Proc. Natl. Acad. Sci. USA
101
4608-4613
2004
Mycobacterium tuberculosis (P9WIN5), Mycobacterium tuberculosis, Mycobacterium tuberculosis ATCC 25618 (P9WIN5)
brenda
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Release 2023.1 (January 2023)
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