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Information on EC 1.14.14.124 - dihydromonacolin L hydroxylase and Organism(s) Aspergillus terreus and UniProt Accession Q9Y7C8

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IUBMB Comments
A cytochrome P-450 (heme-thiolate) protein. The dehydration of 3alpha-hydroxy-3,5-dihydromonacolin L acid is believed to be spontaneous [1,2]. The enzyme from fungi also catalyses the reaction of EC 1.14.14.125, monacolin L hydroxylase .
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Aspergillus terreus
UNIPROT: Q9Y7C8
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The taxonomic range for the selected organisms is: Aspergillus terreus
The enzyme appears in selected viruses and cellular organisms
Synonyms
EC 1.14.13.197, LovA, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SYSTEMATIC NAME
IUBMB Comments
ddihydromonacolin L acid,[reduced NADPH-hemoprotein reductase]:oxygen oxidoreductase (3-hydroxylating)
A cytochrome P-450 (heme-thiolate) protein. The dehydration of 3alpha-hydroxy-3,5-dihydromonacolin L acid is believed to be spontaneous [1,2]. The enzyme from fungi also catalyses the reaction of EC 1.14.14.125, monacolin L hydroxylase [3].
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
3alpha-hydroxy-3,5-dihydromonacolin L acid
monacolin L acid + H2O
show the reaction diagram
spontaneous
(1b), spontaneous
-
?
dihydromonacolin L acid + [reduced NADPH-hemoprotein reductase] + O2
3alpha-hydroxy-3,5-dihydromonacolin L acid + [oxidized NADPH-hemoprotein reductase] + H2O
show the reaction diagram
dihydromonacolin L acid + [reduced NADPH-hemoprotein reductase] + O2
monacolin L acid + [oxidized NADPH-hemoprotein reductase] + H2O
show the reaction diagram
monacolin L acid i.e. (3R,5R)-7-[(1S,2S,6R,8aR)-2,6-dimethyl-1,2,6,7,8,8a-hexahydronaphthalen-1-yl]-3,5-dihydroxyheptanoate. The enzyme also catalyses the reaction of EC 1.14.13.198, monacolin L hydroxylase
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-
?
dihydromonacolin L acid + [reduced NADPH-hemoprotein reductase] + O2
3alpha-hydroxy-3,5-dihydromonacolin L acid + [oxidized NADPH-hemoprotein reductase] + H2O
show the reaction diagram
-
-
product is unstable und under mildly acidic conditions and elevated temperature, it converts to monacolin L
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
dihydromonacolin L acid + [reduced NADPH-hemoprotein reductase] + O2
3alpha-hydroxy-3,5-dihydromonacolin L acid + [oxidized NADPH-hemoprotein reductase] + H2O
show the reaction diagram
dihydromonacolin L acid i.e. (3R,5R)-7-[(1S,2S,4aR,6R,8aS)-2,6-dimethyl-1,2,4a,5,6,7,8,8a-octahydronaphthalen1yl]-3,5-dihydroxyheptanoate. The enzyme also catalyses the reaction of EC 1.14.14.124, monacolin L hydroxylase. The enzyme is involved in the biosynthesis of lovastatin
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-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
cytochrome P-450
a heme-thiolate protein
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
SwissProt
Manually annotated by BRENDA team
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
LOVA_ASPTE
528
0
60593
Swiss-Prot
other Location (Reliability: 5)
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
the lovA gene in C-terminal FLAG-tagged form is cloned in the same vector coding cpr (cytochrome P450 oxidoreductase), and both lovA and cpr are co-expressed in Saccharomyces cerevisiae
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Barriuso, J.; Nguyen, D.T.; Li, J.W.; Roberts, J.N.; MacNevin, G.; Chaytor, J.L.; Marcus, S.L.; Vederas, J.C.; Ro, D.K.
Double oxidation of the cyclic nonaketide dihydromonacolin L to monacolin J by a single cytochrome P450 monooxygenase, LovA
J. Am. Chem. Soc.
133
8078-8081
2011
Aspergillus terreus (Q9Y7C8)
Manually annotated by BRENDA team
Treiber, L.; Reamer, R.; Rooney, C.; Ramjit, H.
Origin of monacolin L from Aspergillus terreus cultures
J. Antibiot.
42
30-36
1989
Aspergillus terreus
Manually annotated by BRENDA team