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Information on EC 1.14.14.125 - monacolin 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 enzyme from fungi also catalyses the reaction of EC 1.14.14.124, dihydromonacolin L hydroxylase.
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This record set is specific for:
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 1.14.13.198, LovA, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SYSTEMATIC NAME
IUBMB Comments
monacolin L acid,[reduced NADPH-hemoprotein reductase]:oxygen oxidoreductase (8-hydroxylating)
A cytochrome P-450 (heme-thiolate) protein. The enzyme from fungi also catalyses the reaction of EC 1.14.14.124, dihydromonacolin L hydroxylase.
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
monacolin L acid + [reduced NADPH-hemoprotein reductase] + O2
monacolin J acid + [oxidized NADPH-hemoprotein reductase] + H2O
show the reaction diagram
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
monacolin L acid + [reduced NADPH-hemoprotein reductase] + O2
monacolin J 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-dihydroxyheptanoic acid. The enzyme also catalyses the reaction of EC 1.14.13.197, dihydromonacolin L hydroxylase. The enzyme is involved in the biosynthesis of lovastatin
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-dihydroxyheptanoic acid
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
cytochrome P-450
a heme-thiolate protein
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0062
monacolin L acid
pH and temperature not specified in the publication
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