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Information on EC 2.3.1.165 - 6-methylsalicylic-acid synthase
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2.3.1.165 6-methylsalicylic-acid synthaseIUBMB Comments
A multienzyme complex with a 4'-phosphopantetheine prosthetic group on the acyl carrier protein. It has a similar sequence to vertebrate type I fatty acid synthase. Acetoacetyl-CoA can also act as a starter molecule.
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Word Map
- 2.3.1.165
-
metropolitan
-
myositis-specific
- autoantibodies
- myositis
- dermatomyositis
-
services
- myopathy
-
census
-
savings
-
subscale
- polymyositis
-
anti-srp
-
anti-mi-2
-
medicare
-
anti-jo-1
- patulum
-
myositis-associated
-
anti-mda5
-
anti-tif1
- mda5
-
microtubule-stabilizing
-
payment
-
amyopathic
-
anti-signal
-
poverty
-
fusimotor
-
cronbach
-
residue-residue
- ketoreductase
-
financing
-
epothilone
-
anti-synthetase
-
alpha-chloralose
-
beneficiaries
-
anti-hmgcr
- food industry
- biotechnology
- synthesis
- medicine
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota
Reaction Schemes
+
3
+
+
=
+
4
+
3
+
+
Synonyms
msas, 6-msa, 6-methylsalicylic acid synthase, iterative type i polyketide synthase, 6-msas, 6-methylsalicylic acid synthetase, chlb1, aomsas, methylsalicylic acid synthase, 6-msa synthase, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
6-methylsalicylic acid synthase
6-MSA
6-MSAS
ASPNIDRAFT_44965
ATX
iPKS
iterative type I polyketide synthase
MSAS
PKS48
YanA
iPKS
-
6-methylsalicylic acid synthase belongs to the iterative type I polyketide synthases (iPKSs), which consist of ketosynthase (KS), acyltransferase (AT), and acyl carrier protein (ACP) domains as a minimum, with additional domains such as ketoreductase (KR), methyltransferase (MeT), and Claisen cyclase (CYC), all on single polypeptides.
iPKS
-
6-methylsalicylic acid synthase belongs to the iterative type I polyketide synthases (iPKSs), which consist of ketosynthase (KS), acyltransferase (AT), and acyl carrier protein (ACP) domains as a minimum, with additional domains such as ketoreductase (KR), methyltransferase (MeT), and Claisen cyclase (CYC), all on single polypeptides.
iterative type I polyketide synthase
-
6-methylsalicylic acid synthase belongs to the iterative type I polyketide synthases (iPKSs), which consist of ketosynthase (KS), acyltransferase (AT), and acyl carrier protein (ACP) domains as a minimum, with additional domains such as ketoreductase (KR), methyltransferase (MeT), and Claisen cyclase (CYC), all on single polypeptides.
iterative type I polyketide synthase
-
6-methylsalicylic acid synthase belongs to the iterative type I polyketide synthases (iPKSs), which consist of ketosynthase (KS), acyltransferase (AT), and acyl carrier protein (ACP) domains as a minimum, with additional domains such as ketoreductase (KR), methyltransferase (MeT), and Claisen cyclase (CYC), all on single polypeptides.
MSAS
-
-
-
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
acetyl-CoA + 3 malonyl-CoA + NADPH + H+ = 6-methylsalicylate + 4 CoA + 3 CO2 + NADP+ + H2O
acetyl-CoA + 3 malonyl-CoA + NADPH + H+ = 6-methylsalicylate + 4 CoA + 3 CO2 + NADP+ + H2O
a multienzyme complex with a 4'-phosphopantetheine prosthetic group on the acyl carrier protein, it has a similar sequence to vertebrate type I fatty acid synthase, acetoacetyl-CoA can also act as a starter molecule
-
acetyl-CoA + 3 malonyl-CoA + NADPH + H+ = 6-methylsalicylate + 4 CoA + 3 CO2 + NADP+ + H2O
steric course of the reaction, mechanism
-
acetyl-CoA + 3 malonyl-CoA + NADPH + H+ = 6-methylsalicylate + 4 CoA + 3 CO2 + NADP+ + H2O
6-methylsalicylate synthesis proceeds without catalytic dehydration of the beta-hydroxy triketide intermediate by DH domain which is therefore not required for tetraketide formation. The subsequent aldol cyclization and aromatization of the tetraketide intermediate then form 6-methylsalicylate covalently bound to the ACP phosphopantetheine arm as the thioester. 6-methylsalicylate is released hydrolytically from ATX by the action of the domain hitherto called DH domain, i.e. the thioester hydrolase catalytic domain
-
acetyl-CoA + 3 malonyl-CoA + NADPH + H+ = 6-methylsalicylate + 4 CoA + 3 CO2 + NADP+ + H2O
a multienzyme complex with a 4'-phosphopantetheine prosthetic group on the acyl carrier protein, it has a similar sequence to vertebrate type I fatty acid synthase, acetoacetyl-CoA can also act as a starter molecule
-
-
acetyl-CoA + 3 malonyl-CoA + NADPH + H+ = 6-methylsalicylate + 4 CoA + 3 CO2 + NADP+ + H2O
-
-
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Claisen condensation
-
-
-
-
reduction
-
-
-
-
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PATHWAY SOURCE
PATHWAYS
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SYSTEMATIC NAME
IUBMB Comments
acyl-CoA:malonyl-CoA C-acyltransferase (decarboxylating, oxoacyl-reducing, thioester-hydrolysing and cyclizing)
A multienzyme complex with a 4'-phosphopantetheine prosthetic group on the acyl carrier protein. It has a similar sequence to vertebrate type I fatty acid synthase. Acetoacetyl-CoA can also act as a starter molecule.
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CAS REGISTRY NUMBER
COMMENTARY
9045-37-8
-
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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
acetoacetyl-CoA + 3 malonyl-CoA + NADPH + H+
6-methyl triacetic acid lactone + CoA + NADP+
-
-
-
?
acetoacetyl-CoA + malonyl-CoA
6-methyl triacetic acid lactone + CoA
-
5% of the rate of 6-methylsalicylic acid synthesis
-
?
acetyl-CoA + malonyl-CoA + NADPH + H+
6-methylsalicylate + CoA + CO2 + NADP+ + H2O
-
-
-
?
butyryl-CoA + malonyl-CoA
6-propyl triacetic acid lactone + CoA
-
5% of the rate of 6-methylsalicylic acid synthesis
-
?
crotonyl-CoA + malonyl-CoA
6-(2-propene) triacetic acid lactone + CoA
-
5% of the rate of 6-methylsalicylic acid synthesis
-
?
heptanoyl-CoA + malonyl-CoA
6-hexyl triacetic acid lactone + CoA
-
5% of the rate of 6-methylsalicylic acid synthesis
-
?
hexanoyl-CoA + malonyl-CoA
6-pentyl triacetic acid lactone + CoA
-
5% of the rate of 6-methylsalicylic acid synthesis
-
?
propionyl-CoA + malonyl-CoA
6-ethyl triacetic acid lactone + CoA
-
5% of the rate of 6-methylsalicylic acid synthesis
-
?
valeryl-CoA + malonyl-CoA
6-butyl triacetic acid lactone + CoA
-
5% of the rate of 6-methylsalicylic acid synthesis
-
?
acetyl-CoA + 3 malonyl-CoA + NADPH + H+
6-methylsalicylate + 4 CoA + 3 CO2 + NADP+ + H2O
-
-
-
-
?
acetyl-CoA + 3 malonyl-CoA + NADPH + H+
6-methylsalicylate + 4 CoA + 3 CO2 + NADP+ + H2O
-
-
-
?
acetyl-CoA + 3 malonyl-CoA + NADPH + H+
6-methylsalicylate + 4 CoA + 3 CO2 + NADP+ + H2O
-
-
-
?
acetyl-CoA + 3 malonyl-CoA + NADPH + H+
6-methylsalicylate + 4 CoA + 3 CO2 + NADP+ + H2O
-
-
-
-
?
acetyl-CoA + 3 malonyl-CoA + NADPH + H+
6-methylsalicylate + 4 CoA + 3 CO2 + NADP+ + H2O
-
ATX by itself can synthesize tetraketide and release 6-methylsalicylate as the free acid without involvement of serine protease-type thioesterase, the product 6-methylsalicylate is retained on the acyl-carrier-protein until its release from ATX, product-releasing mechanism, overview
-
-
?
acetyl-CoA + 3 malonyl-CoA + NADPH + H+
6-methylsalicylate + 4 CoA + 3 CO2 + NADP+ + H2O
-
-
-
?
acetyl-CoA + 3 malonyl-CoA + NADPH + H+
6-methylsalicylate + 4 CoA + 3 CO2 + NADP+ + H2O
-
-
-
?
acetyl-CoA + malonyl-CoA
triacetic lactone
-
exclusive product in the absence of NADPH, 5:1 ratio of 6-methylsalicylic acid to triacetic acid lactone at 0.0005 mM NADPH, less than 1% triacetic acid lactone at 0.012 mM NADPH
-
?
acetyl-CoA + malonyl-CoA
triacetic lactone
-
exclusive product in the absence of NADPH, 5:1 ratio of 6-methylsalicylic acid to triacetic acid lactone at 0.0005 mM NADPH, less than 1% triacetic acid lactone at 0.012 mM NADPH
-
?
acetyl-CoA + malonyl-CoA + NADPH
6-methylsalicylate + CoA + CO2 + NADP+
-
-
-
-
?
acetyl-CoA + malonyl-CoA + NADPH
6-methylsalicylate + CoA + CO2 + NADP+
-
-
-
-
ir
acetyl-CoA + malonyl-CoA + NADPH
6-methylsalicylate + CoA + CO2 + NADP+
-
-
-
?
acetyl-CoA + malonyl-CoA + NADPH
6-methylsalicylate + CoA + CO2 + NADP+
-
-
-
?
acetyl-CoA + malonyl-CoA + NADPH
6-methylsalicylate + CoA + CO2 + NADP+
-
-
-
?
acetyl-CoA + malonyl-CoA + NADPH
6-methylsalicylate + CoA + CO2 + NADP+
-
-
-
?
acetyl-CoA + malonyl-CoA + NADPH
6-methylsalicylate + CoA + CO2 + NADP+
-
-
-
?
acetyl-CoA + malonyl-CoA + NADPH
6-methylsalicylate + CoA + CO2 + NADP+
-
-
-
?
acetyl-CoA + malonyl-CoA + NADPH
6-methylsalicylate + CoA + CO2 + NADP+
-
-
-
?
acetyl-CoA + malonyl-CoA + NADPH
6-methylsalicylate + CoA + CO2 + NADP+
-
-
-
?
acetyl-CoA + malonyl-CoA + NADPH
6-methylsalicylate + CoA + CO2 + NADP+
-
-
-
-
?
acetyl-CoA + malonyl-CoA + NADPH
6-methylsalicylate + CoA + CO2 + NADP+
-
first enzyme of patulin biosynthetic pathway
-
?
acetyl-CoA + malonyl-CoA + NADPH
6-methylsalicylate + CoA + CO2 + NADP+
-
-
-
?
acetyl-CoA + malonyl-CoA + NADPH
6-methylsalicylate + CoA + CO2 + NADP+
-
-
-
?
acetyl-CoA + malonyl-CoA + NADPH
6-methylsalicylate + CoA + CO2 + NADP+
-
first enzyme of patulin biosynthetic pathway
-
?
acetyl-CoA + malonyl-CoA + NADPH
6-methylsalicylate + CoA + CO2 + NADP+
-
-
-
?
acetyl-CoA + pantetheine
acetyl pantetheine + CoA
-
-
-
?
propionyl-CoA + malonyl-CoA + NADPH
6-ethylsalicylate + CoA + CO2 + NADP+
-
-
-
?
propionyl-CoA + malonyl-CoA + NADPH
6-ethylsalicylate + CoA + CO2 + NADP+
-
-
-
?
propionyl-CoA + pantetheine
propionyl pantetheine + CoA
-
13 times slower rate compared to acetyl-CoA
-
?
propionyl-CoA + pantetheine
propionyl pantetheine + CoA
-
13 times slower rate compared to acetyl-CoA
-
?
additional information
?
-
-
the truncated enzyme, THID mutant, hydrolyzes the model substrate 6-methylsalicylic acid-N-acetylcysteamine
-
-
?
additional information
?
-
no enzymatic dehydration takes place at a triketide stage of 6-MSA assembly, so loss of water must occur at the tetraketide stage. The enzyme is able to accept malonate surrogates of different chain lengths and bearing various functionalities (including alkyne and fluorine moieties) at different positions and for every round of chain extension, and also to generate novel pentaketide products
-
-
?
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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
acetyl-CoA + malonyl-CoA + NADPH + H+
6-methylsalicylate + CoA + CO2 + NADP+ + H2O
-
-
-
?
acetyl-CoA + 3 malonyl-CoA + NADPH + H+
6-methylsalicylate + 4 CoA + 3 CO2 + NADP+ + H2O
-
-
-
-
?
acetyl-CoA + 3 malonyl-CoA + NADPH + H+
6-methylsalicylate + 4 CoA + 3 CO2 + NADP+ + H2O
-
-
-
?
acetyl-CoA + malonyl-CoA + NADPH
6-methylsalicylate + CoA + CO2 + NADP+
-
-
-
-
ir
acetyl-CoA + malonyl-CoA + NADPH
6-methylsalicylate + CoA + CO2 + NADP+
-
-
-
?
acetyl-CoA + malonyl-CoA + NADPH
6-methylsalicylate + CoA + CO2 + NADP+
-
first enzyme of patulin biosynthetic pathway
-
?
acetyl-CoA + malonyl-CoA + NADPH
6-methylsalicylate + CoA + CO2 + NADP+
-
-
-
?
acetyl-CoA + malonyl-CoA + NADPH
6-methylsalicylate + CoA + CO2 + NADP+
-
first enzyme of patulin biosynthetic pathway
-
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
5,5'-dithiobis(2-nitrobenzoic acid)
-
0.01 mM, rapid inactivation, inactivation half-life: approx. 15 s, both acetyl-CoA and malonyl-CoA protect
nicotinamide hypoxanthine dinucleotide phosphate
-
reduced form, 0.3 mM, 32% inhibition in crude extracts, oxidized form, 0.3 mM, 24% inhibition in crude extracts
additional information
-
no inhibition by phenylmethylsulfonyl fluoride, a serine protease-type thioesterase inhibitor at 1 mM
-
(2S,3R)-2,3-epoxy-4-oxo-7,10-dodecadienoylamide
-
mycotoxin produced by Cephalosporium caerulens, trivial name cerulenin, 0.2 mM, complete inactivation after approx. 30 min, second-order rate constant for the reaction with 6-methylsalicylic acid synthase: 13.8 M/s, acetyl-CoA protects, site of modification: Cys204
(2S,3R)-2,3-epoxy-4-oxo-7,10-dodecadienoylamide
-
0.0014 mM, complete inactivation after 40 min, acetyl-CoA protects
1,3-dibromo-propane-2-one
-
0.02 mM, complete inactivation after 40 min, acetyl-CoA protects
1,3-dibromo-propane-2-one
-
very rapid inactivation, inactivation half-life: 7 s
iodoacetamide
-
0.5 mM, complete inactivation of synthetase activity after 15 min at 0°C, enzyme is then able to decarboxlate malonyl-CoA
iodoacetamide
-
100 mM, complete inactivation after 45 min, site of modification: Cys204
iodoacetamide
-
100fold molar excess, complete inactivation after 30 min
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
-
in order to activate 6-MSAS a 4'-phosphopantetheinyl transferase, PPTase, is required, therefor a Bacillus subtilis or a Aspergillus nidulans PPTase is coexpressed in yeast
-
additional information
in order to activate 6-MSAS a 4'-phosphopantetheinyl transferase, PPTase, is required, therefor a Bacillus subtilis or a Aspergillus nidulans PPTase is coexpressed in yeast
-
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
5.76
6-Methylsalicylate
-
release from enzyme/acyl-carrier-protein, recombinant His6-tagged THID mutant, pH 7.5, 25°C
12.3
6-Methylsalicylate
-
release from enzyme/acyl-carrier-protein, recombinant His6-tagged ATX, pH 7.5, 25°C
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0125
6-Methylsalicylate
-
release from enzyme/acyl-carrier-protein, recombinant His6-tagged THID mutant, pH 7.5, 25°C
0.023
6-Methylsalicylate
-
release from enzyme/acyl-carrier-protein, recombinant His6-tagged ATX, pH 7.5, 25°C
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
and strains NRRL 5253, NRRL 1678, NRRL 5254, IHEM 3076, MUCL 39714 CBS100.11, NRRL 3849, ATCC 24008
UniProt
brenda
Paecilomyces niveus NRRL 2615
and strains NRRL 5253, NRRL 1678, NRRL 5254, IHEM 3076, MUCL 39714 CBS100.11, NRRL 3849, ATCC 24008
UniProt
brenda
toxigenic Penicillium expansum strain 7015, genome of non-toxigenic strain FV 268 does not contain msas gene
TREMBL
brenda
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
-
6-methylsalicylic acid synthase belongs to the iterative type I polyketide synthases
metabolism
physiological function
metabolism
in toxigenic Penicillium expansum strains msas is involved in the biosynthesis of the mycotoxin patulin which is toxic for animals and plants
metabolism
-
production of 6-methylsalicylic acid as the first step in biosythesis of isoasperlactone and asperlactone
physiological function
-
6-methylsalicylic acid synthase from Aspergillus terreus is not involved in dehydration of the beta-hydroxytriketide intermediate tethered on the acyl carrier protein but catalyzes thioester hydrolysis to release the product from the acyl carrier protein, via its thioester hydrolase domain, a product-releasing domain that is located in the middle of a multidomain iterative type I polyketide synthase, ATX by itself can synthesize tetraketide and release 6-methylsalicylate as the free acid without involvement of serine protease-type thioesterase, product-releasing mechanism, overview
physiological function
enzyme is involved in synthesis of yanuthones D and E
physiological function
-
in Aspergillus aculeatus, 6-methylsalicylic acid is incorporated into aculinic acid, which further incorporates into three compounds named aculins A and B, and epi-aculin A
physiological function
-
enzyme is involved in synthesis of yanuthones D and E
-
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UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). YANA_ASPNA
Aspergillus niger (strain ATCC 1015 / CBS 113.46 / FGSC A1144 / LSHB Ac4 / NCTC 3858a / NRRL 328 / USDA 3528.7)
1779
0
190967
Swiss-Prot
other Location (Reliability: 3)
ACUA_ASPA1
Aspergillus aculeatus (strain ATCC 16872 / CBS 172.66 / WB 5094)
1749
0
187960
Swiss-Prot
other Location (Reliability: 2)
MACA_PENTR
1783
0
190836
Swiss-Prot
other Location (Reliability: 1)
MSAS_PENPA
1774
0
190733
Swiss-Prot
other Location (Reliability: 4)
PATK_PENEN
1776
0
190701
Swiss-Prot
other Location (Reliability: 3)
AR283_ARTOA
Arthrobotrys oligospora (strain ATCC 24927 / CBS 115.81 / DSM 1491)
1761
0
190417
Swiss-Prot
other Location (Reliability: 1)
PATK_ASPCL
Aspergillus clavatus (strain ATCC 1007 / CBS 513.65 / DSM 816 / NCTC 3887 / NRRL 1 / QM 1276 / 107)
1720
0
185005
Swiss-Prot
other Location (Reliability: 2)
ATX_ASPTN
Aspergillus terreus (strain NIH 2624 / FGSC A1156)
1803
0
193794
Swiss-Prot
other Location (Reliability: 1)
A0A0N1GK83_9ACTN
3373
0
352733
TrEMBL
-
A0A0N1GIT2_9ACTN
2792
0
289486
TrEMBL
-
C6C2W0_MUSP7
Musicola paradisiaca (strain Ech703)
2501
0
274572
TrEMBL
-
B2IYN8_NOSP7
Nostoc punctiforme (strain ATCC 29133 / PCC 73102)
1874
0
206708
TrEMBL
-
A0A831A0Z5_ERWAM
1734
0
187857
TrEMBL
-
A0A084GE65_PSEDA
2671
0
291005
TrEMBL
other Location (Reliability: 1)
Q3M5Z5_TRIV2
Trichormus variabilis (strain ATCC 29413 / PCC 7937)
1874
0
206183
TrEMBL
-
F0SIS4_RUBBR
Rubinisphaera brasiliensis (strain ATCC 49424 / DSM 5305 / JCM 21570 / IAM 15109 / NBRC 103401 / IFAM 1448)
2672
0
290156
TrEMBL
-
A0A840QGF5_9PSEU
1730
0
182698
TrEMBL
-
A0A5K1JTR6_9APHY
192
0
21877
TrEMBL
other Location (Reliability: 5)
K0K2V5_SACES
Saccharothrix espanaensis (strain ATCC 51144 / DSM 44229 / JCM 9112 / NBRC 15066 / NRRL 15764)
1702
0
179747
TrEMBL
-
A0A5K1K5T4_9APHY
605
0
66932
TrEMBL
Secretory Pathway (Reliability: 4)
A0A0N0MSL3_9ACTN
3920
0
409143
TrEMBL
-
A0A1L7F9W4_9PSEU
1735
0
184206
TrEMBL
-
A0A841BTG7_9ACTN
1731
0
182316
TrEMBL
-
A0A840QFW0_9PSEU
1613
0
168400
TrEMBL
-
A0A840Q359_9PSEU
1699
0
177721
TrEMBL
-
B2J539_NOSP7
Nostoc punctiforme (strain ATCC 29133 / PCC 73102)
1897
0
207689
TrEMBL
-
A0A852V3M1_9ACTN
1901
0
194493
TrEMBL
-