Information on EC 2.1.1.237 - mycinamicin III 3''-O-methyltransferase

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The expected taxonomic range for this enzyme is: Micromonospora griseorubida

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EC NUMBER
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2.1.1.237
preliminary BRENDA-supplied EC number
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RECOMMENDED NAME
GeneOntology No.
mycinamicin III 3''-O-methyltransferase
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REACTION
REACTION DIAGRAM
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ORGANISM
UNIPROT
LITERATURE
S-adenosyl-L-methionine + mycinamicin III = S-adenosyl-L-homocysteine + mycinamicin IV
show the reaction diagram
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
mycinamicin biosynthesis
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Biosynthesis of antibiotics
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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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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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GENERAL INFORMATION
ORGANISM
UNIPROT
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LITERATURE
evolution
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structural basis of substrate specificity and regiochemistry in the MycF/TylF family of sugar O-methyltransferases, overview
malfunction
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construction of a MycF disrupion mutant. The disruption mutant mainly produces mycinamicin III
metabolism
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the 3'-O-methyltransferase enzyme is involved in the biosynthesis of the macrolide antibiotic mycinamicin
physiological function
additional information
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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
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SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
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LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
S-adenosyl-L-methionine + mycinamicin III
S-adenosyl-L-homocysteine + mycinamicin IV
show the reaction diagram
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NATURAL SUBSTRATES
NATURAL PRODUCTS
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 + mycinamicin III
S-adenosyl-L-homocysteine + mycinamicin IV
show the reaction diagram
-
the enzyme is involved in the biosynthesis of mycinamicin macrolide antibiotics
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-
?
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COFACTOR
ORGANISM
UNIPROT
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LITERATURE
IMAGE
S-adenosyl-L-methionine
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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
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LITERATURE
Co2+
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activation is about 90% of the activation obtained by Mg2+
Fe2+
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activation is about 70% of the activation obtained by Mg2+; activation is about 90% of the activation obtained by Mg2+
Mg2+
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optimal activity in presence of 10 mM MgCl2
Mn2+
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activation is about equal to the activation obtained by Mg2+
Zn2+
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activation is about equal to the activation obtained by Mg2+
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INHIBITORS
ORGANISM
UNIPROT
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LITERATURE
IMAGE
additional information
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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 hide
LITERATURE
IMAGE
0.0307
mycinamicin III
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pH 7.4, 30°C
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.225
mycinamicin III
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pH 7.4, 30°C
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
7.3
mycinamicin III
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pH 7.4, 30°C
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
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LITERATURE
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PDB
SCOP
CATH
UNIPROT
ORGANISM
Micromonospora griseorubida;
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
28600
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28600, SDS-PAGE
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SUBUNITS
ORGANISM
UNIPROT
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LITERATURE
?
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28600, SDS-PAGE
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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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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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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
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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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APPLICATION
ORGANISM
UNIPROT
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LITERATURE
medicine
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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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LINKS TO OTHER DATABASES (specific for EC-Number 2.1.1.237)
ExplorEnz
ExPASy
KEGG
MetaCyc
SABIO-RK
NCBI: PubMed, Protein, Nucleotide, Structure, Genome, OMIM
IUBMB Enzyme Nomenclature
PROSITE Database of protein families and domains
InterPro (database of protein families, domains and functional sites)