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Information on EC 2.3.1.161 - lovastatin nonaketide synthase and Organism(s) Aspergillus terreus and UniProt Accession Q9Y8A5
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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 taxonomic range for the selected organisms is: Aspergillus terreus
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota
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
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
LNKS
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
reaction mechanism
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
decarboxylation
cyclization
reduction
dehydration
decarboxylation
-
-
-
-
cyclization
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-
-
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reduction
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-
-
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dehydration
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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.
CAS REGISTRY NUMBER
COMMENTARY
235426-97-8
-
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 + 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
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
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 + 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
-
-
?
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.
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-
ir
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
-
-
?
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 + 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
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
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 + 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
-
-
?
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
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
enzyme utilizes an oxidized quinone as cofactor
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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
-
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
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
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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
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)
PDB
SCOP
CATH
UNIPROT
ORGANISM
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
335000
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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
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
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
the single domains are purified using Ni-nitrilotriacetic agarose resin and anion-exchange chromatography
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
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+
minimal polyketide synthase domains of subunit LovB as standalone proteins
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
medicine
lovastatin is a fungal polyketide metabolite produced by Aspergillus terreus that has been used as a drug to lower cholesterol levels
medicine
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
-
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
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
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
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
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)
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)
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
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
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)
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)
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