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Information on EC 2.3.1.238 - monacolin J acid methylbutanoate transferase
for references in articles please use BRENDA:EC2.3.1.238
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EC Tree 2 Transferases
2.3 Acyltransferases
2.3.1 Transferring groups other than aminoacyl groups
2.3.1.238 monacolin J acid methylbutanoate transferase
IUBMB Comments
The enzyme catalyses the ultimate reaction in the lovastatin biosynthesis pathway of the filamentous fungus Aspergillus terreus.
The enzyme appears in viruses and cellular organisms
Reaction Schemes
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(S)-2-methylbutanoyl-[2-methylbutanoate polyketide synthase]
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[2-methylbutanoate polyketide synthase]
Synonyms
LovD, more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
LovD
LovD
-
-
-
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
monacolin J acid + (S)-2-methylbutanoyl-[2-methylbutanoate polyketide synthase] = lovastatin acid + [2-methylbutanoate polyketide synthase]
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PATHWAY SOURCE
PATHWAYS
MetaCyc
lovastatin biosynthesis
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SYSTEMATIC NAME
IUBMB Comments
monacolin J acid:(S)-2-methylbutanoyl-[2-methylbutanoate polyketide synthase] (S)-2-methylbutanoate transferase
The enzyme catalyses the ultimate reaction in the lovastatin biosynthesis pathway of the filamentous fungus Aspergillus terreus.
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
(S)-2-methylbutanoyl-N-acetylcysteamine + 6-hydroxy-6-demethylmonacolin J
pravastatin + N-acetylcysteamine
Substrates: -
Products: -
Products: -
?
(S)-2-methylbutanoyl-N-acetylcysteamine + monacolin J
lovastatin + N-acetylcysteamine
Substrates: -
Products: -
Products: -
?
alpha-dimethylbutanoyl-N-acetylcysteamine + 6-hydroxy-6-demethylmonacolin J
huvastatin + N-acetylcysteamine
Substrates: -
Products: -
Products: -
?
alpha-dimethylbutanoyl-N-acetylcysteamine + monacolin J
simvastatin + N-acetylcysteamine
Substrates: -
Products: -
Products: -
?
alpha-dimethylbutanoyl-N-acetylcysteamine + monacolin J acid
simvastatin + N-acetylcysteamine
Substrates: -
Products: -
Products: -
?
butanoyl-N-acetylcysteamine + monacolin J
(1S,3R,7S,8S,8aR)-8-[2-[(2R,4R)-4-hydroxy-6-oxotetrahydro-2H-pyran-2-yl]ethyl]-3,7-dimethyl-1,2,3,7,8,8a-hexahydronaphthalen-1-yl butanoate + N-acetylcysteamine
Substrates: -
Products: -
Products: -
?
butyryl-CoA + monacolin J
(1S,3R,7S,8S,8aR)-8-[2-[(2R,4R)-4-hydroxy-6-oxotetrahydro-2H-pyran-2-yl]ethyl]-3,7-dimethyl-1,2,3,7,8,8a-hexahydronaphthalen-1-yl butanoate + CoA
Substrates: 87% conversion after 10 h
Products: -
Products: -
?
hexanoyl-N-acetylcysteamine + monacolin J
? + N-acetylcysteamine
Substrates: -
Products: -
Products: -
?
monacolin J acid + (S)-2-methylbutanoyl-[2-methylbutanoate polyketide synthase]
lovastatin acid + [2-methylbutanoate polyketide synthase]
pentanoyl-N-acetylcysteamine + monacolin J
? + N-acetylcysteamine
Substrates: -
Products: -
Products: -
?
monacolin J acid + (S)-2-methylbutanoyl-[2-methylbutanoate polyketide synthase]
lovastatin acid + [2-methylbutanoate polyketide synthase]
Substrates: -
Products: -
Products: -
?
monacolin J acid + (S)-2-methylbutanoyl-[2-methylbutanoate polyketide synthase]
lovastatin acid + [2-methylbutanoate polyketide synthase]
Substrates: the enzyme is involved in lovastatin biosynthesis
Products: -
Products: -
?
monacolin J acid + (S)-2-methylbutanoyl-[2-methylbutanoate polyketide synthase]
lovastatin acid + [2-methylbutanoate polyketide synthase]
Substrates: monacolin J acid i.e. (3R,5R)-7-[(1S,2S,6R,8S,8aR)-8-hydroxy-2,6-dimethyl-1,2,6,7,8,8a-hexahydronaphthalen-1-yl]-3,5-dihydroxyheptanoate
Products: lovastatin acid i.e. (3R,5R)-7-[(1S,2S,6R,8S,8aR)-2,6-dimethyl-8-[[(2S)-2-methylbutanoyl]oxy]-1,2,6,7,8,8a-hexahydronaphthalen-1-yl]-3,5-dihydroxyheptanoate
Products: lovastatin acid i.e. (3R,5R)-7-[(1S,2S,6R,8S,8aR)-2,6-dimethyl-8-[[(2S)-2-methylbutanoyl]oxy]-1,2,6,7,8,8a-hexahydronaphthalen-1-yl]-3,5-dihydroxyheptanoate
?
monacolin J acid + (S)-2-methylbutanoyl-[2-methylbutanoate polyketide synthase]
lovastatin acid + [2-methylbutanoate polyketide synthase]
Substrates: the enzyme primarily interacts with the ACP domain of 2-methylbutanoate polyketide synthase (LovF) and the protein-protein interactions leads to highly efficient transfer of the diketide product
Products: -
Products: -
?
additional information
?
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Substrates: the enzyme displays preference toward medium chain length (C3C6) acyl groups, with butyryl-CoA being the optimal alkylacyl-CoA substrate. Both acetyl- and octanoyl-CoA are poor substrates of LovD, with less than 10% acylation of monacolin J. The enzyme also catalyzes hydrolysis of lovastain to monacolin J. Butyryl-thioethane and butyryl-thioethanol are not competent substrates of the enzyme
Products: -
Products: -
?
additional information
?
-
Substrates: LovD displays two competitive catalytic capabilities: thioesterase (unproductive hydrolysis alpha-dimethylbutanoyl-N-acetylcysteamine) and acyltransferase (productive acyl transfer from alpha-dimethylbutanoyl-N-acetylcysteamine to monacolin J acid)
Products: -
Products: -
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
monacolin J acid + (S)-2-methylbutanoyl-[2-methylbutanoate polyketide synthase]
lovastatin acid + [2-methylbutanoate polyketide synthase]
monacolin J acid + (S)-2-methylbutanoyl-[2-methylbutanoate polyketide synthase]
lovastatin acid + [2-methylbutanoate polyketide synthase]
Substrates: -
Products: -
Products: -
?
monacolin J acid + (S)-2-methylbutanoyl-[2-methylbutanoate polyketide synthase]
lovastatin acid + [2-methylbutanoate polyketide synthase]
Substrates: the enzyme is involved in lovastatin biosynthesis
Products: -
Products: -
?
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
monacolin J
competitive inhibitor of butyryl-CoA, substrate inhibition occurs due to binding of monacolin J to the free enzyme, forming a LovD-monacolin J complex and blocking entrance of butyryl-CoA
additional information
no substrate inhibition by butyryl-CoA at high concentrations is observed
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.039
(S)-2-methylbutanoyl-[2-methylbutanoate polyketide synthase]
pH and temperature not specified in the publication
-
additional information
additional information
Km-value for hydrolysis of lovastain to monacolin J is 0.56 mM
-
0.6
monacolin J acid
mutant I4N/A9V/K26E/R28S/I35L/N43R/D96R/S109C/A123P/M157V/S164G/S172N/L174F/A178L/N191G/L192I/Q241M/A247S/R250K/S256T/A261H/G275S/Q297G/L335M/L361M/V370I/A383V/N391S/H404K, pH not specified in the publication, temperature not specified in the publication
4.2
monacolin J acid
wild-type, pH not specified in the publication, temperature not specified in the publication
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.806
(S)-2-methylbutanoyl-[2-methylbutanoate polyketide synthase]
pH and temperature not specified in the publication
-
additional information
additional information
kcat-value for hydrolysis of lovastain to monacolin J is 0.0035/s
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0.004
monacolin J acid
wild-type, pH not specified in the publication, temperature not specified in the publication
0.29
monacolin J acid
mutant I4N/A9V/K26E/R28S/I35L/N43R/D96R/S109C/A123P/M157V/S164G/S172N/L174F/A178L/N191G/L192I/Q241M/A247S/R250K/S256T/A261H/G275S/Q297G/L335M/L361M/V370I/A383V/N391S/H404K, 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
20.7
(S)-2-methylbutanoyl-[2-methylbutanoate polyketide synthase]
pH and temperature not specified in the publication
-
0.0009
monacolin J acid
wild-type, pH not specified in the publication, temperature not specified in the publication
0.451
monacolin J acid
mutant I4N/A9V/K26E/R28S/I35L/N43R/D96R/S109C/A123P/M157V/S164G/S172N/L174F/A178L/N191G/L192I/Q241M/A247S/R250K/S256T/A261H/G275S/Q297G/L335M/L361M/V370I/A383V/N391S/H404K, pH not specified in the publication, temperature not specified in the publication
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
8.4
monacolin J acid
mutant I4N/A9V/K26E/R28S/I35L/N43R/D96R/S109C/A123P/M157V/S164G/S172N/L174F/A178L/N191G/L192I/Q241M/A247S/R250K/S256T/A261H/G275S/Q297G/L335M/L361M/V370I/A383V/N391S/H404K, pH not specified in the publication, temperature not specified in the publication
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pH OPTIMUM
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
Highest Expressing Human Cell Lines
Cell Line LinksPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
physiological function
the enzyme is involved in lovastatin biosynthesis
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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). LOVD_ASPTN
Aspergillus terreus (strain NIH 2624 / FGSC A1156)
413
0
46056
Swiss-Prot
-
MOKF_MONPI
413
1
46693
Swiss-Prot
Secretory Pathway (Reliability: 1)
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
I4N/A9V/K26E/R28S/I35L/N43R/D96R/S109C/A123P/M157V/S164G/S172N/L174F/A178L/N191G/L192I/Q241M/A247S/R250K/S256T/A261H/G275S/Q297G/L335M/L361M/V370I/A383V/N391S/H404K
mutant LovD9, engineered variant for synthesis of simvastatin. LovD9 shows the highest kcat/KM and Ki values of all variants studied
S76A
additional information
buried and substrate entrance channel mutation clusters are the major contributors to the activity enhancement in LovD variants. Mutations at buried positions largely favor the acyl transfer over acyl-enzyme complex hydrolysis, while mutations at the substrate entrance channel mitigate the inevitable product hydrolysis. Combination of variants of the clusters has a cumulative effect
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
synthesis
the enzyme can be a useful biocatalyst for the synthesis of simvastatin and other statin analogs. It is an attractive enzyme for engineered biosynthesis of pharmaceutically important cholesterol-lowering drugs
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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 (Q9Y7D1)
brenda
Xie, X.; Watanabe, K.; Wojcicki, W.A.; Wang, C.C.; Tang, Y.
Biosynthesis of lovastatin analogs with a broadly specific acyltransferase
Chem. Biol.
13
1161-1169
2006
Aspergillus terreus (Q9Y7D1)
brenda
Xie, X.; Meehan, M.J.; Xu, W.; Dorrestein, P.C.; Tang, Y.
Acyltransferase mediated polyketide release from a fungal megasynthase
J. Am. Chem. Soc.
131
8388-8389
2009
Aspergillus terreus (Q9Y7D1)
brenda
Garcia-Marquina, G.; Nunez-Franco, R.; Peccati, F.; Tang, Y.; Jimenez-Oses, G.; Lopez-Gallego, F.
Deconvoluting the directed evolution pathway of engineered acyltransferase LovD
ChemCatChem
14
e202101345
2022
Aspergillus terreus (Q9Y7D1)
-
brenda
EXTERNAL LINKS (specific for EC-Number 2.3.1.238)
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