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Information on EC 2.1.1.239 - L-olivosyl-oleandolide 3-O-methyltransferase and Organism(s) Streptomyces antibioticus and UniProt Accession O87833

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IUBMB Comments
The enzyme is involved in the biosynthesis of the macrolide antibiotic oleandomycin in Streptomyces antibioticus. It can also act on other monoglycosylated macrolactones, including L-rhamnosyl-erythronolide B and L-mycarosyl-erythronolide B.
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This record set is specific for:
Streptomyces antibioticus
UNIPROT: O87833
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The taxonomic range for the selected organisms is: Streptomyces antibioticus
The enzyme appears in selected viruses and cellular organisms
Synonyms
OleY, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SYSTEMATIC NAME
IUBMB Comments
S-adenosyl-L-methionine:L-olivosyl-oleandolide B 3-O-methyltransferase
The enzyme is involved in the biosynthesis of the macrolide antibiotic oleandomycin in Streptomyces antibioticus. It can also act on other monoglycosylated macrolactones, including L-rhamnosyl-erythronolide B and L-mycarosyl-erythronolide B.
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
S-adenosyl-L-methionine + L-mycarosyl-erythronolide B
S-adenosyl-L-homocysteine + ?
show the reaction diagram
poor substrate
-
-
?
S-adenosyl-L-methionine + L-olivosyl-erythronolide B
S-adenosyl-L-homocysteine + L-oleandrosyl-erythronolide B
show the reaction diagram
S-adenosyl-L-methionine + L-rhamnosyl-erythronolide B
S-adenosyl-L-homocysteine + ?
show the reaction diagram
-
-
-
?
additional information
?
-
no bioconversion is observed when other glycosylated macrolide antibiotics (spiramycin, niddamycin, carbomycin) are added to cultures of Streptomyces albus NAG2(pLR14b-4). These three macrolides contain L-mycarose moieties with a free 3-hydroxy group but are not methylated by OleY
-
-
?
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
S-adenosyl-L-methionine + L-olivosyl-erythronolide B
S-adenosyl-L-homocysteine + L-oleandrosyl-erythronolide B
show the reaction diagram
the enzyme is involved in biosynthesis of the macrolide antibiotic oleandomycin
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Co2+
0.1 mM, 11fold stimulation of activity
Fe2+
0.1 mM, 1.5fold stimulation of activity
Mg2+
0.1 mM, 3.5fold stimulation of activity
Mn2+
0.1 mM, 7fold stimulation of activity
Zn2+
0.1 mM, 5fold stimulation of activity
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
Cu2+
0.1 mM, strong inhibition
EDTA
1 mM, strong inhibition
Hg2+
0.1 mM, strong inhibition
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.00000256
pH 8.0, 30°C
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.5 - 7.8
pH 6.5: about 60% of maximal activity, pH 7.8: about 60% of maximal activity
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
OLEY_STRAT
386
0
42439
Swiss-Prot
-
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
43000
2 * 43000, SDS-PAGE
87000
gel filtration
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
dimer
2 * 43000, SDS-PAGE
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-70°C, enzyme keeps most of the activity after 30 days
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
overexpression in Escherichia coli as inclusion bodies and in Streptomyces lividans or Streptomyces albus as soluble protein
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Rodrguez, L.; Rodrguez, D.; Olano, C.; Brana, A.F.; Mendez, C.; Salas, J.A.
Functional analysis of OleY L-oleandrosyl 3-O-methyltransferase of the oleandomycin biosynthetic pathway in Streptomyces antibioticus
J. Bacteriol.
183
5358-5363
2001
Streptomyces antibioticus (O87833)
Manually annotated by BRENDA team