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Enzyme Nomenclature
Information on EC 2.3.1.252 - mycolipanoate synthase
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The expected taxonomic range for this enzyme is: Bacteria, Eukaryota
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EC NUMBER 
COMMENTARY 
2.3.1.252
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RECOMMENDED NAME
GeneOntology No.
mycolipanoate synthase
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
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
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
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SYSTEMATIC NAME
IUBMB Comments
long-chain acyl-CoA: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.
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
malfunction
malfunction
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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
malfunction
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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
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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
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
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
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-
-
?
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
the 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
mycolipanoic acid i.e. (2S,4S,6S)-2,4,6-trimethyl-very-long-chain fatty acid
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?
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
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-
-
?
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
the 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
mycolipanoic acid i.e. (2S,4S,6S)-2,4,6-trimethyl-very-long-chain fatty acid
-
?
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NATURAL SUBSTRATES
NATURAL PRODUCTS
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
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
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
P9WQE9
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-
-
?
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
P9WQE9
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-
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?
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
220300
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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
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
phosphorylated PhoP directly stimulates transcription of the enzyme (45fold)
phosphorylated PhoP directly stimulates transcription of the enzyme (45fold)
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phosphorylated PhoP directly stimulates transcription of the enzyme (45fold)
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LINKS TO OTHER DATABASES (specific for EC-Number 2.3.1.252)
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