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Information on EC 2.1.1.237 - mycinamicin III 3''-O-methyltransferase
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2.1.1.237 mycinamicin III 3''-O-methyltransferaseIUBMB Comments
The enzyme is involved in the biosynthesis of mycinamicin macrolide antibiotics.
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The enzyme appears in viruses and cellular organisms
Reaction Schemes
Synonyms
MycF, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
MycF
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
S-adenosyl-L-methionine + mycinamicin III = S-adenosyl-L-homocysteine + mycinamicin IV
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-
-
-
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PATHWAY SOURCE
PATHWAYS
MetaCyc
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SYSTEMATIC NAME
IUBMB Comments
S-adenosyl-L-methionine:mycinamicin III 3''-O-methyltransferase
The enzyme is involved in the biosynthesis of mycinamicin macrolide antibiotics.
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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
S-adenosyl-L-methionine + mycinamicin III
S-adenosyl-L-homocysteine + mycinamicin IV
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-
-
-
?
S-adenosyl-L-methionine + mycinamicin III
S-adenosyl-L-homocysteine + mycinamicin IV
-
the enzyme is involved in the biosynthesis of mycinamicin macrolide antibiotics
-
-
?
S-adenosyl-L-methionine + mycinamicin III
S-adenosyl-L-homocysteine + mycinamicin IV
-
methylation of the C3''-OH of javose. Mycf possesses high substrate specificity. MycE is methylating mycinamycin VI
-
-
?
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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
S-adenosyl-L-methionine + mycinamicin III
S-adenosyl-L-homocysteine + mycinamicin IV
-
the enzyme is involved in the biosynthesis of mycinamicin macrolide antibiotics
-
-
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
S-adenosyl-L-methionine
cofacor binding induces substantial ordering that creates the binding site for the natural substrate, and a bound metal ion positions the substrate for catalysis
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Co2+
-
activation is about 90% of the activation obtained by Mg2+
Fe2+
Mn2+
-
activation is about equal to the activation obtained by Mg2+
Zn2+
-
activation is about equal to the activation obtained by Mg2+
Fe2+
-
activation is about 70% of the activation obtained by Mg2+
Fe2+
-
activation is about 90% of the activation obtained by Mg2+
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
-
addition of 2 mM of EDTA fails to abrogate activity, suggesting that a metal ion might be dispensible in the O-methyltransferase reaction catalysed by MycF
-
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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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
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
physiological function
malfunction
-
construction of a MycF disrupion mutant. The disruption mutant mainly produces mycinamicin III
metabolism
the 3'-O-methyltransferase enzyme is involved in the biosynthesis of the macrolide antibiotic mycinamicin
evolution
structural basis of substrate specificity and regiochemistry in the MycF/TylF family of sugar O-methyltransferases, overview
additional information
using the MycF substrate complex and the modeled substrate complex of a 4'-specific homologue, active site residues were identified that correlate with the 3' or 4' specificity of MycF family members and define the protein and substrate features that direct the regiochemistry of methyltransfer
physiological function
-
the enzyme is involved in the biosynthesis of mycinamicin macrolide antibiotics. Mycinamicins represent a family of macrolide antibiotics with more than twenty members produced by the rare actinomycete Micromonospora griseorubida
physiological function
S-adenosyl-L-methionine cofacor binding induces substantial ordering that creates the binding site for the natural substrate, and a bound metal ion positions the substrate for catalysis
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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). A0A1V4XHR2_9DELT
279
0
31521
TrEMBL
-
A0A1J5RMD9_9ZZZZ
357
0
38874
TrEMBL
other Location (Reliability: 1)
A0A1V5F7L0_9BACT
244
0
26759
TrEMBL
-
A0A1C3NXL1_9ACTN
279
0
31632
TrEMBL
-
A0A1V5ZM57_9BACT
192
0
22150
TrEMBL
-
A0A1V6GIB2_9BACT
242
0
27793
TrEMBL
-
A0A6B9B718_MYCAV
275
0
30949
TrEMBL
-
A0A1V4WUV2_9DELT
259
0
30068
TrEMBL
-
A0A6L5BR06_9PSED
240
0
27161
TrEMBL
-
A0A6B9B868_MYCAV
266
0
30046
TrEMBL
-
A0A0S4HYW7_9PSED
240
0
27190
TrEMBL
-
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PDB
SCOP
CATH
UNIPROT
ORGANISM
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
analysis of crystal structures of MycF, including the free enzyme and complexes with S-adenosyl homocysteine, substrate, product, and unnatural substrates
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
a single amino acid substitution relaxes the 2'-methoxy specificity but retains regiospecificity. The engineered variant produces a new mycinamicin analogue, demonstrating the utility of structural information to facilitate bioengineering approaches for the chemoenzymatic synthesis of complex small molecules containing modified sugars
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant N-terminal His6-tagged protein, purified by one-step Ni-NTA agarose chromatography
-
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
MycF is cloned into pET28b for overexpression in Escherichia coli BL21 (DE3)
-
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
medicine
-
the antibacterial activities of some mycinamicin products against Staphylococcus aureus are higher than those of clinical macrolide antibiotics erythromycin and leucomycin
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Li, S.; Anzai, Y.; Kinoshita, K.; Kato, F.; Sherman, D.H.
Functional analysis of MycE and MycF, two O-methyltransferases involved in the biosynthesis of mycinamicin macrolide antibiotics
Chembiochem
10
1297-1301
2009
Micromonospora griseorubida
brenda
Anzai, Y.; Saito, N.; Tanaka, M.; Kinoshita, K.; Koyama, Y.; Kato, F.
Organization of the biosynthetic gene cluster for the polyketide macrolide mycinamicin in Micromonospora griseorubida
FEMS Microbiol. Lett.
218
135-141
2003
Micromonospora griseorubida (Q49492), Micromonospora griseorubida A11725 (Q49492)
brenda
Tsukada, S.; Anzai, Y.; Li, S.; Kinoshita, K.; Sherman, D.H.; Kato, F.
Gene targeting for O-methyltransferase genes, mycE and mycF, on the chromosome of Micromonospora griseorubida producing mycinamicin with a disruption cassette containing the bacteriophage phi C31 attB attachment site
FEMS Microbiol. Lett.
304
148-156
2010
Micromonospora griseorubida
brenda
Bernard, S.M.; Akey, D.L.; Tripathi, A.; Park, S.R.; Konwerski, J.R.; Anzai, Y.; Li, S.; Kato, F.; Sherman, D.H.; Smith, J.L.
Structural basis of substrate specificity and regiochemistry in the MycF/TylF family of sugar O-methyltransferases
ACS Chem. Biol.
10
1340-1351
2015
Micromonospora griseorubida (Q49492)
brenda
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