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Information on EC 2.3.1.161 - lovastatin nonaketide synthase
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EC Tree
2.3.1.161 lovastatin nonaketide synthaseIUBMB Comments
This fungal enzyme system comprises a multi-functional polyketide synthase (PKS) and an enoyl reductase. The PKS catalyses many of the chain building reactions of EC 2.3.1.85, fatty-acid synthase system, as well as a reductive methylation and a Diels-Alder reaction, while the reductase is responsible for three enoyl reductions that are necessary for dihydromonacolin L acid production.
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Word Map
- 2.3.1.161
- polyketide
-
iterative
- synthases
- terreus
- medicine
-
enoyl
-
megasynthase
-
cholesterol-lowering
- s-adenosylmethionine
-
diketide
- 2-methylbutyrate
- pyrones
-
transesterase
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota
Reaction Schemes
9
+
11
+
10
+
+
=
+
9
+
9
+
11
+
+
6
9
+
11
+
10
+
+
holo-[lovastatin nonaketide synthase]
=
dihydromonacolin L-[lovastatin nonaketide synthase]
+
9
+
9
+
11
+
+
6
Synonyms
lovastatin nonaketide synthase, 
more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
LNKS
lovastatin nonaketide synthase
LovB
synthase, lovastatin nonaketide
-
-
-
-
LNKS
-
-
-
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
9 malonyl-CoA + 11 NADPH + 10 H+ + S-adenosyl-L-methionine + holo-[lovastatin nonaketide synthase] = dihydromonacolin L-[lovastatin nonaketide synthase] + 9 CoA + 9 CO2 + 11 NADP+ + S-adenosyl-L-homocysteine + 6 H2O
9 malonyl-CoA + 11 NADPH + 10 H+ + S-adenosyl-L-methionine + holo-[lovastatin nonaketide synthase] = dihydromonacolin L-[lovastatin nonaketide synthase] + 9 CoA + 9 CO2 + 11 NADP+ + S-adenosyl-L-homocysteine + 6 H2O
reaction mechanism
-
9 malonyl-CoA + 11 NADPH + 10 H+ + S-adenosyl-L-methionine + holo-[lovastatin nonaketide synthase] = dihydromonacolin L-[lovastatin nonaketide synthase] + 9 CoA + 9 CO2 + 11 NADP+ + S-adenosyl-L-homocysteine + 6 H2O
-
-
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
cyclization
decarboxylation
dehydration
reduction
cyclization
-
-
-
-
decarboxylation
-
-
-
-
dehydration
-
-
-
-
reduction
-
-
-
-
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PATHWAY SOURCE
PATHWAYS
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SYSTEMATIC NAME
IUBMB Comments
acyl-CoA:malonyl-CoA C-acyltransferase (dihydromonacolin L acid-forming)
This fungal enzyme system comprises a multi-functional polyketide synthase (PKS) and an enoyl reductase. The PKS catalyses many of the chain building reactions of EC 2.3.1.85, fatty-acid synthase system, as well as a reductive methylation and a Diels-Alder reaction, while the reductase is responsible for three enoyl reductions that are necessary for dihydromonacolin L acid production.
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CAS REGISTRY NUMBER
COMMENTARY
235426-97-8
-
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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
(4E,6E)-2-methyl-3-oxoocta-4,6-dienoyl-S-ACP + NADPH + H+
(4E,6E)-2-methyl-3-hydroxyocta-4,6-dienoyl-S-ACP + NADP+
reaction of ketoreductase subunit, natural substrate. ACP = acyl-carrier protein
-
-
?
(4E,6E)-3-oxoocta-4,6-dienoyl-N-acetylcysteamine + S-adenosyl-L-methionine
(4E,6E)-2-methyl-3-oxoocta-4,6-dienoyl-N-acetylcysteamine + S-adenosyl-L-homocysteine
reaction of methyltransferase subunit, natural substrate analogue. ACP = acyl-carrier protein
-
-
?
(4E,6E)-3-oxoocta-4,6-dienoyl-S-ACP + S-adenosyl-L-methionine
(4E,6E)-2-methyl-3-oxoocta-4,6-dienoyl-S-ACP + S-adenosyl-L-homocysteine
reaction of methyltransferase subunit, natural substrate. ACP = acyl-carrier protein
-
-
?
2-methyl-3-oxohexanoyl-N-acetylcysteamine + NADPH + H+
3-hydroxy-2-methylhexanoyl-N-acetylcysteamine + NADP+
reaction of ketoreductase subunit, natural substrate
-
-
?
3-oxohexanoyl-N-acetylcysteamine + NADPH + H+
3-hydroxyhexanoyl-N-acetylcysteamine + NADP+
reaction of ketoreductase subunit, natural substrate
-
-
?
3-oxooctanoyl-N-acetylcysteamine + S-adenosyl-L-methionine
2-methyl-3-oxooctanoyl-N-acetylcysteamine + S-adenosyl-L-homocysteine
reaction of methyltransferase subunit, artificial substrate. 0.3% of the activity with (4E,6E)-3-oxoocta-4,6-dienoyl-N-acetylcysteamine
-
-
?
acetyl-CoA + 8 malonyl-CoA + 11 NADPH + S-adenosyl-L-methionine + 11 H+
dihydromonacolin L + 9 CoA + 8 CO2 + 11 NADP+ + S-adenosyl-L-homocysteine + 6 H2O
acetyl-CoA + malonyl-CoA + NADPH + H+ + S-adenosyl-L-methionine
4-hydroxy-6-[(1E,3E,5E)-1-methylhepta-1,3,5-trien-1-yl]-2H-pyran-2-one + 4-hydroxy-6-[(1E,3E,5E,7E)-3-methylnona-1,3,5,7-tetraen-1-yl]-2H-pyran-2-one + CoA + CO2 + NADP+ + S-adenosyl-L-homocysteine + H2O
-
in absence of accessory protein LovC, formation of truncated pyrones 4-hydroxy-6-[(1E,3E,5E)-1-methylhepta-1,3,5-trien-1-yl]-2H-pyran-2-one + 4-hydroxy-6-[(1E,3E,5E,7E)-3-methylnona-1,3,5,7-tetraen-1-yl]-2H-pyran-2-one. Chemical synthesis of these truncated pyrones for analysis of enzyme reaction
-
?
acetyl-CoA + malonyl-CoA + NADPH + H+ + S-adenosyl-L-methionine
?
in the absence of the accessory protein LovC, LovB forms conjugated pyrones as truncated polyketide synthase products
-
-
?
acetyl-CoA + malonyl-CoA + NADPH + H+ + S-adenosyl-L-methionine
dihydromonacolin L + CoA + CO2 + NADP+ + S-adenosyl-L-homocysteine + H2O
additional information
?
-
the methyltransferase domain displays methylation activity toward different beta-ketoacyl groups, it is exceptionally selective toward its naturally programmed beta-keto-dienyltetraketide substrate with respect to both chain length and functionalization. The ketoreductase domain displays broader substrate specificity toward different beta-ketoacyl groups
-
-
?
acetyl-CoA + 8 malonyl-CoA + 11 NADPH + S-adenosyl-L-methionine + 11 H+
dihydromonacolin L + 9 CoA + 8 CO2 + 11 NADP+ + S-adenosyl-L-homocysteine + 6 H2O
-
reaction mechanism
-
-
?
acetyl-CoA + 8 malonyl-CoA + 11 NADPH + S-adenosyl-L-methionine + 11 H+
dihydromonacolin L + 9 CoA + 8 CO2 + 11 NADP+ + S-adenosyl-L-homocysteine + 6 H2O
-
enzyme contains six active sites: ketosynthase, acyltransferase, dehydratase, enoyl reductase, ketoreductase and acyl carrier protein
-
-
?
acetyl-CoA + 8 malonyl-CoA + 11 NADPH + S-adenosyl-L-methionine + 11 H+
dihydromonacolin L + 9 CoA + 8 CO2 + 11 NADP+ + S-adenosyl-L-homocysteine + 6 H2O
-
enzyme contains six active sites: ketosynthase, acyltransferase, dehydratase, enoyl reductase, ketoreductase and acyl carrier protein
-
?
acetyl-CoA + 8 malonyl-CoA + 11 NADPH + S-adenosyl-L-methionine + 11 H+
dihydromonacolin L + 9 CoA + 8 CO2 + 11 NADP+ + S-adenosyl-L-homocysteine + 6 H2O
-
enzyme also displays Diels-Alderase activity in vitro
-
?
acetyl-CoA + 8 malonyl-CoA + 11 NADPH + S-adenosyl-L-methionine + 11 H+
dihydromonacolin L + 9 CoA + 8 CO2 + 11 NADP+ + S-adenosyl-L-homocysteine + 6 H2O
-
enzyme also displays Diels-Alderase activity in vitro
-
-
?
acetyl-CoA + 8 malonyl-CoA + 11 NADPH + S-adenosyl-L-methionine + 11 H+
dihydromonacolin L + 9 CoA + 8 CO2 + 11 NADP+ + S-adenosyl-L-homocysteine + 6 H2O
-
reaction mechanism, interaction with LovC
-
-
?
acetyl-CoA + 8 malonyl-CoA + 11 NADPH + S-adenosyl-L-methionine + 11 H+
dihydromonacolin L + 9 CoA + 8 CO2 + 11 NADP+ + S-adenosyl-L-homocysteine + 6 H2O
-
reaction mechanism, enzyme interacts with LovC to catalyze 35 separate reactions in the biosynthesis of dihydrononacolin
-
-
?
acetyl-CoA + 8 malonyl-CoA + 11 NADPH + S-adenosyl-L-methionine + 11 H+
dihydromonacolin L + 9 CoA + 8 CO2 + 11 NADP+ + S-adenosyl-L-homocysteine + 6 H2O
-
accessory protein LovC is needed: Loading of the megasynthase by malonyl-CoA is presumably followed by decarboxylation to yield the acetyl starter unit. Each round of Claisen condensation is catalyzed by the KS domain, whereas the growing polyketide is tethered to the phosphopantetheinyl arm of the ACP. After each condensation, the polyketide is subjected to a different combination of tailoring, which can include alpha-methylation by the MT domain, beta-ketoreduction by the KR domain, beta-dehydration by the DH domain, and alpha-beta-enoylreduction by the dissociated LovC. The different tailoring permutations after each round of chain extension yield a triene-containing hexaketide thioester that can undergo a stereospecific Diels-Alder cyclization to yield the decalin portion. After formation of the nonaketide, the chain is released to yield the ring-open form. In the absence of LovC, methylated hexa- and heptaketide pyrones are the primary products.
-
-
ir
acetyl-CoA + malonyl-CoA + NADPH + H+ + S-adenosyl-L-methionine
dihydromonacolin L + CoA + CO2 + NADP+ + S-adenosyl-L-homocysteine + H2O
-
-
-
?
acetyl-CoA + malonyl-CoA + NADPH + H+ + S-adenosyl-L-methionine
dihydromonacolin L + CoA + CO2 + NADP+ + S-adenosyl-L-homocysteine + H2O
-
in presence of accessory protein LovC, formation of dihydrononacolin C
-
?
acetyl-CoA + malonyl-CoA + NADPH + H+ + S-adenosyl-L-methionine
dihydromonacolin L + CoA + CO2 + NADP+ + S-adenosyl-L-homocysteine + H2O
-
reaction catalyzed by Lov B + Loc C. Mutant disruoted at the lovC gene lacks the ability to produce dihydrononacolin L
-
-
?
acetyl-CoA + malonyl-CoA + NADPH + H+ + S-adenosyl-L-methionine
dihydromonacolin L + CoA + CO2 + NADP+ + S-adenosyl-L-homocysteine + H2O
in the presence of the accessory protein LovC
-
-
?
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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
(4E,6E)-2-methyl-3-oxoocta-4,6-dienoyl-S-ACP + NADPH + H+
(4E,6E)-2-methyl-3-hydroxyocta-4,6-dienoyl-S-ACP + NADP+
reaction of ketoreductase subunit, natural substrate. ACP = acyl-carrier protein
-
-
?
(4E,6E)-3-oxoocta-4,6-dienoyl-S-ACP + S-adenosyl-L-methionine
(4E,6E)-2-methyl-3-oxoocta-4,6-dienoyl-S-ACP + S-adenosyl-L-homocysteine
reaction of methyltransferase subunit, natural substrate. ACP = acyl-carrier protein
-
-
?
2-methyl-3-oxohexanoyl-N-acetylcysteamine + NADPH + H+
3-hydroxy-2-methylhexanoyl-N-acetylcysteamine + NADP+
reaction of ketoreductase subunit, natural substrate
-
-
?
3-oxohexanoyl-N-acetylcysteamine + NADPH + H+
3-hydroxyhexanoyl-N-acetylcysteamine + NADP+
reaction of ketoreductase subunit, natural substrate
-
-
?
acetyl-CoA + 8 malonyl-CoA + 11 NADPH + S-adenosyl-L-methionine + 11 H+
dihydromonacolin L + 9 CoA + 8 CO2 + 11 NADP+ + S-adenosyl-L-homocysteine + 6 H2O
acetyl-CoA + malonyl-CoA + NADPH + H+ + S-adenosyl-L-methionine
?
in the absence of the accessory protein LovC, LovB forms conjugated pyrones as truncated polyketide synthase products
-
-
?
acetyl-CoA + malonyl-CoA + NADPH + H+ + S-adenosyl-L-methionine
dihydromonacolin L + CoA + CO2 + NADP+ + S-adenosyl-L-homocysteine + H2O
additional information
?
-
the methyltransferase domain displays methylation activity toward different beta-ketoacyl groups, it is exceptionally selective toward its naturally programmed beta-keto-dienyltetraketide substrate with respect to both chain length and functionalization. The ketoreductase domain displays broader substrate specificity toward different beta-ketoacyl groups
-
-
?
acetyl-CoA + 8 malonyl-CoA + 11 NADPH + S-adenosyl-L-methionine + 11 H+
dihydromonacolin L + 9 CoA + 8 CO2 + 11 NADP+ + S-adenosyl-L-homocysteine + 6 H2O
-
reaction mechanism
-
-
?
acetyl-CoA + 8 malonyl-CoA + 11 NADPH + S-adenosyl-L-methionine + 11 H+
dihydromonacolin L + 9 CoA + 8 CO2 + 11 NADP+ + S-adenosyl-L-homocysteine + 6 H2O
-
reaction mechanism, interaction with LovC
-
-
?
acetyl-CoA + 8 malonyl-CoA + 11 NADPH + S-adenosyl-L-methionine + 11 H+
dihydromonacolin L + 9 CoA + 8 CO2 + 11 NADP+ + S-adenosyl-L-homocysteine + 6 H2O
-
reaction mechanism, enzyme interacts with LovC to catalyze 35 separate reactions in the biosynthesis of dihydrononacolin
-
-
?
acetyl-CoA + malonyl-CoA + NADPH + H+ + S-adenosyl-L-methionine
dihydromonacolin L + CoA + CO2 + NADP+ + S-adenosyl-L-homocysteine + H2O
-
-
-
?
acetyl-CoA + malonyl-CoA + NADPH + H+ + S-adenosyl-L-methionine
dihydromonacolin L + CoA + CO2 + NADP+ + S-adenosyl-L-homocysteine + H2O
in the presence of the accessory protein LovC
-
-
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
enzyme utilizes an oxidized quinone as cofactor
-
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.17
(4E,6E)-3-oxoocta-4,6-dienoyl-N-acetylcysteamine
pH not specified in the publication, temperature not specified in the publication
2
3-oxohexanoyl-N-acetylcysteamine
pH not specified in the publication, temperature not specified in the publication
5.2
3-oxooctanoyl-N-acetylcysteamine
pH not specified in the publication, temperature not specified in the publication
additional information
additional information
-
in absence of accessory protein LovC, enzyme forms truncated pyrones 4-hydroxy-6-[(1E,3E,5E)-1-methylhepta-1,3,5-trien-1-yl]-2H-pyran-2-one + 4-hydroxy-6-[(1E,3E,5E,7E)-3-methylnona-1,3,5,7-tetraen-1-yl]-2H-pyran-2-one. Chemical synthesis of these truncated pyrones for analysis of enzyme reaction
-
additional information
additional information
in absence of accessory protein LovC, enzyme forms truncated pyrones 4-hydroxy-6-[(1E,3E,5E)-1-methylhepta-1,3,5-trien-1-yl]-2H-pyran-2-one + 4-hydroxy-6-[(1E,3E,5E,7E)-3-methylnona-1,3,5,7-tetraen-1-yl]-2H-pyran-2-one. Chemical synthesis of these truncated pyrones for analysis of enzyme reaction
-
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
3.25
(4E,6E)-3-oxoocta-4,6-dienoyl-N-acetylcysteamine
pH not specified in the publication, temperature not specified in the publication
0.085
2-methyl-3-oxohexanoyl-N-acetylcysteamine
pH not specified in the publication, temperature not specified in the publication
0.57
3-oxohexanoyl-N-acetylcysteamine
pH not specified in the publication, temperature not specified in the publication
0.32
3-oxooctanoyl-N-acetylcysteamine
pH not specified in the publication, temperature not specified in the publication
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
18.93
(4E,6E)-3-oxoocta-4,6-dienoyl-N-acetylcysteamine
pH not specified in the publication, temperature not specified in the publication
0.31
3-oxohexanoyl-N-acetylcysteamine
pH not specified in the publication, temperature not specified in the publication
0.06
3-oxooctanoyl-N-acetylcysteamine
pH not specified in the publication, temperature not specified in the publication
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SPECIFIC ACTIVITY [µmol/min/mg]
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
release of reaction product from enzyme LovB is mediated by multifunctional esterase LovG. LovG is also involved in the clearance of aberrant intermediates from LovB
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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). LOVB_ASPTE
3038
0
335005
Swiss-Prot
other Location (Reliability: 2)
LOVB_ASPTN
Aspergillus terreus (strain NIH 2624 / FGSC A1156)
3038
0
335023
Swiss-Prot
other Location (Reliability: 2)
LOVC_ASPTE
363
0
39511
Swiss-Prot
other Location (Reliability: 2)
LOVC_ASPTN
Aspergillus terreus (strain NIH 2624 / FGSC A1156)
363
0
39442
Swiss-Prot
other Location (Reliability: 2)
MOKA_MONPI
3075
0
338037
Swiss-Prot
other Location (Reliability: 5)
B8MLL4_TALSN
Talaromyces stipitatus (strain ATCC 10500 / CBS 375.48 / QM 6759 / NRRL 1006)
2434
0
267301
TrEMBL
other Location (Reliability: 2)
B8MJ47_TALSN
Talaromyces stipitatus (strain ATCC 10500 / CBS 375.48 / QM 6759 / NRRL 1006)
2574
0
283293
TrEMBL
other Location (Reliability: 1)
B8MM59_TALSN
Talaromyces stipitatus (strain ATCC 10500 / CBS 375.48 / QM 6759 / NRRL 1006)
2528
0
277252
TrEMBL
other Location (Reliability: 2)
A0A0F4YNJ2_TALEM
2507
0
275906
TrEMBL
other Location (Reliability: 3)
B8MKY6_TALSN
Talaromyces stipitatus (strain ATCC 10500 / CBS 375.48 / QM 6759 / NRRL 1006)
2570
0
280373
TrEMBL
other Location (Reliability: 2)
A0A0F4YWL7_TALEM
2441
0
268479
TrEMBL
other Location (Reliability: 3)
B9PYE4_TOXGV
Toxoplasma gondii (strain ATCC 50861 / VEG)
10021
0
1093469
TrEMBL
other Location (Reliability: 4)
A0A125YWR9_TOXGM
Toxoplasma gondii (strain ATCC 50611 / Me49)
10021
0
1093469
TrEMBL
other Location (Reliability: 4)
A0A425HS93_TOXGO
4935
0
537026
TrEMBL
other Location (Reliability: 4)
A0A1S8AAC1_ROSNE
287
0
30835
TrEMBL
other Location (Reliability: 1)
B8MMZ2_TALSN
Talaromyces stipitatus (strain ATCC 10500 / CBS 375.48 / QM 6759 / NRRL 1006)
944
0
104780
TrEMBL
other Location (Reliability: 2)
A0A3R8B0H5_TOXGO
3206
0
351058
TrEMBL
other Location (Reliability: 2)
A0A0F4Z407_TALEM
2645
0
290259
TrEMBL
other Location (Reliability: 1)
A0A086PSR3_TOXGO
4874
0
530255
TrEMBL
other Location (Reliability: 4)
A0A086JT50_TOXGO
4874
0
530301
TrEMBL
other Location (Reliability: 4)
B8MSF8_TALSN
Talaromyces stipitatus (strain ATCC 10500 / CBS 375.48 / QM 6759 / NRRL 1006)
2621
0
292309
TrEMBL
other Location (Reliability: 1)
A0A086QNR6_TOXGO
3127
0
342267
TrEMBL
other Location (Reliability: 1)
B8M9X6_TALSN
Talaromyces stipitatus (strain ATCC 10500 / CBS 375.48 / QM 6759 / NRRL 1006)
2388
0
259340
TrEMBL
other Location (Reliability: 2)
A0A1S8A8I9_ROSNE
372
0
40054
TrEMBL
Mitochondrion (Reliability: 3)
A0A0F8B1C0_CERFI
1215
0
132247
TrEMBL
other Location (Reliability: 2)
A0A139XLM1_TOXGO
4958
0
539630
TrEMBL
other Location (Reliability: 4)
A0A086JYW5_TOXGO
4402
0
479141
TrEMBL
other Location (Reliability: 2)
B8M7V1_TALSN
Talaromyces stipitatus (strain ATCC 10500 / CBS 375.48 / QM 6759 / NRRL 1006)
2347
0
254045
TrEMBL
other Location (Reliability: 1)
A0A084GE65_PSEDA
2671
0
291005
TrEMBL
other Location (Reliability: 1)
A0A086LSF6_TOXGO
8102
0
884254
TrEMBL
other Location (Reliability: 3)
B8MSM2_TALSN
Talaromyces stipitatus (strain ATCC 10500 / CBS 375.48 / QM 6759 / NRRL 1006)
2368
0
257448
TrEMBL
other Location (Reliability: 1)
B8M0G9_TALSN
Talaromyces stipitatus (strain ATCC 10500 / CBS 375.48 / QM 6759 / NRRL 1006)
2432
0
264836
TrEMBL
other Location (Reliability: 3)
A0A0F4YEG7_TALEM
2638
0
291086
TrEMBL
other Location (Reliability: 1)
A0A2G8XS11_TOXGO
2195
1
239077
TrEMBL
Secretory Pathway (Reliability: 4)
B8M2A8_TALSN
Talaromyces stipitatus (strain ATCC 10500 / CBS 375.48 / QM 6759 / NRRL 1006)
3725
0
413131
TrEMBL
other Location (Reliability: 1)
A0A125YWR8_TOXGG
Toxoplasma gondii (strain ATCC 50853 / GT1)
10021
0
1093469
TrEMBL
other Location (Reliability: 4)
A0A086KQL2_TOXGO
4874
0
530301
TrEMBL
other Location (Reliability: 4)
B8MV59_TALSN
Talaromyces stipitatus (strain ATCC 10500 / CBS 375.48 / QM 6759 / NRRL 1006)
2521
0
274036
TrEMBL
other Location (Reliability: 1)
B8MPC7_TALSN
Talaromyces stipitatus (strain ATCC 10500 / CBS 375.48 / QM 6759 / NRRL 1006)
3928
0
433762
TrEMBL
other Location (Reliability: 2)
A0A2G8XS22_TOXGO
3330
0
364582
TrEMBL
other Location (Reliability: 1)
A0A086JT20_TOXGO
3127
0
342267
TrEMBL
other Location (Reliability: 1)
B8MFT5_TALSN
Talaromyces stipitatus (strain ATCC 10500 / CBS 375.48 / QM 6759 / NRRL 1006)
2436
0
268706
TrEMBL
other Location (Reliability: 2)
B8MP12_TALSN
Talaromyces stipitatus (strain ATCC 10500 / CBS 375.48 / QM 6759 / NRRL 1006)
2652
0
293187
TrEMBL
other Location (Reliability: 2)
A0A086PST4_TOXGO
3206
0
351147
TrEMBL
other Location (Reliability: 2)
A0A0N1G602_9ACTN
1519
0
166318
TrEMBL
-
B8MQ32_TALSN
Talaromyces stipitatus (strain ATCC 10500 / CBS 375.48 / QM 6759 / NRRL 1006)
2493
0
274764
TrEMBL
other Location (Reliability: 2)
A0A1S8A5D8_ROSNE
146
0
16604
TrEMBL
other Location (Reliability: 3)
A0A086QNT2_TOXGO
4874
0
530301
TrEMBL
other Location (Reliability: 4)
B8MPF4_TALSN
Talaromyces stipitatus (strain ATCC 10500 / CBS 375.48 / QM 6759 / NRRL 1006)
2515
0
275859
TrEMBL
other Location (Reliability: 2)
A0A086KQG0_TOXGO
3127
0
342267
TrEMBL
other Location (Reliability: 1)
B8MEL0_TALSN
Talaromyces stipitatus (strain ATCC 10500 / CBS 375.48 / QM 6759 / NRRL 1006)
2900
0
319164
TrEMBL
other Location (Reliability: 2)
B8MEK8_TALSN
Talaromyces stipitatus (strain ATCC 10500 / CBS 375.48 / QM 6759 / NRRL 1006)
2289
0
251996
TrEMBL
other Location (Reliability: 2)
A0A139XLM6_TOXGO
3311
0
362462
TrEMBL
other Location (Reliability: 3)
A0A2G8XT12_TOXGO
2629
0
284960
TrEMBL
other Location (Reliability: 2)
A0A086JYV0_TOXGO
3288
0
360081
TrEMBL
other Location (Reliability: 3)
B8MPM4_TALSN
Talaromyces stipitatus (strain ATCC 10500 / CBS 375.48 / QM 6759 / NRRL 1006)
3968
0
439115
TrEMBL
other Location (Reliability: 2)
B8LWY1_TALSN
Talaromyces stipitatus (strain ATCC 10500 / CBS 375.48 / QM 6759 / NRRL 1006)
2262
0
248927
TrEMBL
other Location (Reliability: 2)
A0A0F4YYJ7_TALEM
2439
0
265318
TrEMBL
other Location (Reliability: 2)
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PDB
SCOP
CATH
UNIPROT
ORGANISM
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
335000
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
S656A
additional information
S656A
inactivation of malonyl-coenzyme A:acyl carrier protein acyltransferase domain in ketosynthase-malonyl-coenzyme A:acyl carrier protein acyltransferase for assay of ketosynthase activity. Ketosynthase displays no activity towards acetyl groups but recognizes malonyl groups in the absence of cerulenin
additional information
-
expression of minimal polyketide synthase domains of subunit LovB as standalone proteins. The didomain proteins ketosynthase-malonyl-coenzyme A:acyl carrier protein acyltransferase KS-MAT can transfer the acyl group to both the cognate LovB acyl carrier protein and heterologous acyl carrier proteins from bacterial type I and type II polyketide synthases. It transfers malonyl and acetyl groups with kcat/Km values of 0.62 per min and 0.032 per min, resp
additional information
expression of minimal polyketide synthase domains of subunit LovB as standalone proteins. The didomain proteins ketosynthase-malonyl-coenzyme A:acyl carrier protein acyltransferase KS-MAT can transfer the acyl group to both the cognate LovB acyl carrier protein and heterologous acyl carrier proteins from bacterial type I and type II polyketide synthases. It transfers malonyl and acetyl groups with kcat/Km values of 0.62 per min and 0.032 per min, resp
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
the single domains are purified using Ni-nitrilotriacetic agarose resin and anion-exchange chromatography
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
minimal polyketide synthase domains of subunit LovB as standalone proteins
the entire lovB gene is inserted into pET21a+ to create pSMa33, the LovB KS-MAT didomain, MAT, ACP, ACP-CON and CON are each amplified from pSMa33 and cloned into pET28a+
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
medicine
medicine
lovastatin is a fungal polyketide metabolite produced by Aspergillus terreus that has been used as a drug to lower cholesterol levels
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Auclair, K.; Sutherland, A.; Kennedy, J.; Witter, D.J.; Van den Heever, J.P.; Hutchinson, C.R.; Vederas, J.C.
Lovastatin nonaketide synthase catalyzes an intramolecular Diels-Alder reaction of a substrate analogue
J. Am. Chem. Soc.
122
11519-11520
2000
Aspergillus terreus
-
brenda
Hendrickson, L.; Davis, C.R.; Roach, C.; Nguyen, D.K.; Aldrich, T.; McAda, P.C.; Reeves, C.D.
Lovastatin biosynthesis in Aspergillus terreus: characterization of blocked mutants, enzyme activities and a multifunctional polyketide synthase gene
Chem. Biol.
6
429-439
1999
Aspergillus terreus
brenda
Hutchinson, C.R.; Kennedy, J.; Park, C.; Kendrew, S.; Auclair, K.; Vederas, J.
Aspects of the biosynthesis of non-aromatic fungal polyketides by iterative polyketide synthases
Antonie van Leeuwenhoek
78
287-295
2000
Aspergillus terreus
brenda
Kennedy, J.; Auclair, K.; Kendrew, S.G.; Park, C.; Vederas, J.C.; Hutchinson, C.R.
Modulation of polyketide synthase activity by accessory proteins during lovastatin biosynthesis
Science
284
1368-1372
1999
Aspergillus terreus
brenda
Sorensen, J.L.; Auclair, K.; Kennedy, J.; Hutchinson, C.R.; Vederas, J.C.
Transformations of cyclic nonaketides by Aspergillus terreus mutants blocked for lovastatin biosynthesis at the lovA and lovC genes
Org. Biomol. Chem.
1
50-59
2003
Aspergillus terreus
brenda
Ma, S.M.; Tang, Y.
Biochemical characterization of the minimal polyketide synthase domains in the lovastatin nonaketide synthase LovB
FEBS J.
274
2854-2864
2007
Aspergillus terreus, Aspergillus terreus (Q9Y8A5)
brenda
Burr, D.A.; Chen, X.B.; Vederas, J.C.
Syntheses of conjugated pyrones for the enzymatic assay of lovastatin nonaketide synthase, an iterative polyketide synthase
Org. Lett.
9
161-164
2007
Aspergillus terreus, Aspergillus terreus (Q9Y8A5)
brenda
Lee, K.K.; Da Silva, N.A.; Kealey, J.T.
Determination of the extent of phosphopantetheinylation of polyketide synthases expressed in Escherichia coli and Saccharomyces cerevisiae
Anal. Biochem.
394
75-80
2009
Aspergillus terreus
brenda
Ma, S.M.; Li, J.W.; Choi, J.W.; Zhou, H.; Lee, K.K.; Moorthie, V.A.; Xie, X.; Kealey, J.T.; Da Silva, N.A.; Vederas, J.C.; Tang, Y.
Complete reconstitution of a highly reducing iterative polyketide synthase
Science
326
589-592
2009
Aspergillus terreus
brenda
Xu, W.; Chooi, Y.; Choi, J.; Li, S.; Vederas, J.; Da Silva, N.; Tang, Y.
LovG: The thioesterase required for dihydromonacolin L release and lovastatin nonaketide synthase turnover in lovastatin biosynthesis
Angew. Chem. Int. Ed. Engl.
52
6472-6475
2013
Aspergillus terreus (Q9Y8A5)
brenda
Cacho, R.A.; Thuss, J.; Xu, W.; Sanichar, R.; Gao, Z.; Nguyen, A.; Vederas, J.C.; Tang, Y.
Understanding programming of fungal iterative polyketide synthases: the biochemical basis for regioselectivity by the methyltransferase domain in the lovastatin megasynthase
J. Am. Chem. Soc.
137
15688-15691
2015
Aspergillus terreus (Q9Y8A5)
brenda
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