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Information on EC 2.1.1.304 - L-tyrosine C3-methyltransferase and Organism(s) Streptomyces lavendulae and UniProt Accession B0CN31

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EC Tree
     2 Transferases
         2.1 Transferring one-carbon groups
             2.1.1 Methyltransferases
                2.1.1.304 L-tyrosine C3-methyltransferase
IUBMB Comments
The enzyme from the bacterium Streptomyces lavendulae is involved in biosynthesis of saframycin A, a potent antitumor antibiotic that belongs to the tetrahydroisoquinoline family.
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This record set is specific for:
Streptomyces lavendulae
UNIPROT: B0CN31
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The taxonomic range for the selected organisms is: Streptomyces lavendulae
The enzyme appears in selected viruses and cellular organisms
Synonyms
sfmm2, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
PATHWAY SOURCE
PATHWAYS
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SYSTEMATIC NAME
IUBMB Comments
S-adenosyl-L-methionine:L-tyrosine C3-methyltransferase
The enzyme from the bacterium Streptomyces lavendulae is involved in biosynthesis of saframycin A, a potent antitumor antibiotic that belongs to the tetrahydroisoquinoline family.
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 + D-tyrosine
S-adenosyl-L-homocysteine + 3-methyl-D-tyrosine
show the reaction diagram
24% of the activity as compared to L-tyrosine
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-
?
S-adenosyl-L-methionine + L-tyrosine
S-adenosyl-L-homocysteine + 3-methyl-L-tyrosine
show the reaction diagram
additional information
?
-
activity with L-DOPA is 1% of the activity with L-tyrosine
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-
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-tyrosine
S-adenosyl-L-homocysteine + 3-methyl-L-tyrosine
show the reaction diagram
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
heme
a heme containing protein. The conserved motif HXXXC is crucial for heme binding. SfmD binds one molecular of heme
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
SFMM2_STRLA
366
0
39990
Swiss-Prot
-
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
41800
x * 41800, SDS-PAGE
42000
x * 42000, SDS-PAGE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli K12
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Tang, M.C.; Fu, C.Y.; Tang, G.L.
Characterization of SfmD as a heme peroxidase that catalyzes the regioselective hydroxylation of 3-methyltyrosine to 3-hydroxy-5-methyltyrosine in saframycin A biosynthesis
J. Biol. Chem.
287
5112-5121
2012
Streptomyces lavendulae (B0CN31), Streptomyces lavendulae NRRL 11002 (B0CN31)
Manually annotated by BRENDA team
Fu, C.Y.; Tang, M.C.; Peng, C.; Li, L.; He, Y.L.; Liu, W.; Tang, G.L.
Biosynthesis of 3-hydroxy-5-methyl-o-methyltyrosine in the saframycin/safracin biosynthetic pathway
J. Microbiol. Biotechnol.
19
439-446
2009
Streptomyces lavendulae (B0CN31), Streptomyces lavendulae
Manually annotated by BRENDA team
Tengg, M.; Stecher, H.; Offner, L.; Plasch, K.; Anderl, F.; Weber, H.; Schwab, H.; Gruber-Khadjawi, M.
Methyltransferases green catalysts for Friedel-Crafts alkylations
ChemCatChem
8
1354-1360
2016
Pseudomonas fluorescens, Streptomyces lavendulae (B0CN31)
-
Manually annotated by BRENDA team