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Information on EC 2.3.1.252 - mycolipanoate synthase and Organism(s) Mycobacterium tuberculosis and UniProt Accession P9WQE9

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EC Tree
     2 Transferases
         2.3 Acyltransferases
             2.3.1 Transferring groups other than aminoacyl groups
                2.3.1.252 mycolipanoate synthase
IUBMB Comments
This mycobacterial enzyme accepts long-chain fatty acyl groups from their CoA esters and extends them by incorporation of three methylmalonyl (but not malonyl) residues, forming trimethyl-branched fatty-acids such as (2S,4S,6S)-2,4,6-trimethyltetracosanoate (C27-mycolipanoate). Since the enzyme lacks a thioesterase domain, the product remains bound to the enzyme and requires additional enzyme(s) for removal.
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This record set is specific for:
Mycobacterium tuberculosis
UNIPROT: P9WQE9
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The taxonomic range for the selected organisms is: Mycobacterium tuberculosis
The expected taxonomic range for this enzyme is: Mycobacterium
Reaction Schemes
hide
a long-chain acyl-CoA
+
3
(S)-methylmalonyl-CoA
+
6
NADPH
+
6
H+
+
holo-[mycolipanoate synthase]
=
mycolipanoyl-[mycolipanoate synthase]
+
4
CoA
+
3
CO2
+
6
NADP+
+
3
H2O
+
3
+
6
+
6
+
holo-[mycolipanoate synthase]
=
mycolipanoyl-[mycolipanoate synthase]
+
4
+
3
+
6
+
3
Synonyms
Msl3, Pks2, pks3, polyketide beta-ketoacyl synthase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
polyketide beta-ketoacyl synthase
-
-
PATHWAY SOURCE
PATHWAYS
-
-
SYSTEMATIC NAME
IUBMB Comments
long-chain acyl-CoA:(S)-methylmalonyl-CoA C-acyltransferase (mycolipanoate-forming)
This mycobacterial enzyme accepts long-chain fatty acyl groups from their CoA esters and extends them by incorporation of three methylmalonyl (but not malonyl) residues, forming trimethyl-branched fatty-acids such as (2S,4S,6S)-2,4,6-trimethyltetracosanoate (C27-mycolipanoate). Since the enzyme lacks a thioesterase domain, the product remains bound to the enzyme and requires additional enzyme(s) for removal.
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
a long-chain acyl-CoA + 3 (R)-methylmalonyl-CoA + 6 NADPH + 6 H+ + holo-[mycolipanoate synthase]
mycolipanoyl-[mycolipanoate synthase] + 4 CoA + 3 CO2 + 6 NADP+ + 3 H2O
show the reaction diagram
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
a long-chain acyl-CoA + 3 (R)-methylmalonyl-CoA + 6 NADPH + 6 H+ + holo-[mycolipanoate synthase]
mycolipanoyl-[mycolipanoate synthase] + 4 CoA + 3 CO2 + 6 NADP+ + 3 H2O
show the reaction diagram
-
-
-
?
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malfunction
Msl3 is disrupted using a phage mediated delivery system. Biochemical analysis shows that the msl3 mutant does not produce mycolipanoic acids and mycolipenic (phthienoic) acids, the major constituents of polyacyl trehaloses and thus lacks this cell wall lipid, but synthesizes all of the other classes of lipids. The absence of the major acyl chains that anchor the surface-exposed acyltrehaloses causes a novel growth morphology. The cells stick to each other, most probably via the intercellular interaction between the exposed hydrophobic cell surfaces, manifesting a bead-like growth morphology without affecting the overall growth rate
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
220300
calculated from sequence of pks3 and pks4. The genes originally designated pks3 and pks4 in Mycobacterium tuberculosis genome jointly constitute a single gene (msl3) encoding a 220000 Da protein
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
phosphorylated PhoP directly stimulates transcription of the enzyme (45fold)
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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 (P9WQE9), Mycobacterium tuberculosis ATCC 25618 (P9WQE9)
Manually annotated by BRENDA team
Goyal, R.; Das, A.K.; Singh, R.; Singh, P.K.; 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 (A0A089QRB9), Mycobacterium tuberculosis H37Rv (A0A089QRB9)
Manually annotated by BRENDA team
Dubey, V.S.; Sirakova, T.D.; Kolattukudy, P.E.
Disruption of msl3 abolishes the synthesis of mycolipanoic and mycolipenic acids required for polyacyltrehalose synthesis in Mycobacterium tuberculosis H37Rv and causes cell aggregation
Mol. Microbiol.
45
1451-1459
2002
Mycobacterium tuberculosis (A0A089QRB9), Mycobacterium tuberculosis H37Rv (A0A089QRB9)
Manually annotated by BRENDA team
Walters, S.B.; Dubnau, E.; Kolesnikova, I.; Laval, F.; Daffe, M.; Smith, I.
The Mycobacterium tuberculosis PhoPR two-component system regulates genes essential for virulence and complex lipid biosynthesis
Mol. Microbiol.
60
312-330
2006
Mycobacterium tuberculosis, Mycobacterium tuberculosis H37Rv
Manually annotated by BRENDA team