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Information on EC 2.1.1.235 - dTDP-3-amino-3,6-dideoxy-alpha-D-glucopyranose N,N-dimethyltransferase for references in articles please use BRENDA:EC2.1.1.235Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
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The expected taxonomic range for this enzyme is: Streptomyces fradiae
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dTDP-3-amino-3,6-dideoxy-alpha-D-glucopyranose N,N-dimethyltransferase
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2 S-adenosyl-L-methionine + dTDP-3-amino-3,6-dideoxy-alpha-D-glucopyranose = 2 S-adenosyl-L-homocysteine + dTDP-3-dimethylamino-3,6-dideoxy-alpha-D-glucopyranose
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dTDP-alpha-D-mycaminose biosynthesis
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Polyketide sugar unit biosynthesis
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Biosynthesis of antibiotics
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S-adenosyl-L-methionine:dTDP-3-amino-3,6-dideoxy-alpha-D-glucopyranose 3-N,N-dimethyltransferase
The enzyme is involved in the biosynthesis of mycaminose, an essential structural component of the macrolide antibiotic tylosin, which is produced by the bacterium Streptomyces fradiae.
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UniProt
brenda
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additional information
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structure model of TylM1 with bound S-adenosyl-L-methionine and dTDP-phenol: Model of the Michaelis complex in stereo. The C-3' amino group is positioned to attack the methyl group of S-adenoyl-L-methionine. dTDP-mycaminose binding pocket structure, overview
physiological function
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the enzyme catalyzes the N,N-dimethylation step in the biosynthesis of mycaminose. Mycaminose is an aminohexose found in several macrolide antibiotics. The sugar contains a C-3 N,N-dimethylamino group which confers the biological activity of these unusual sugar
physiological function
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the enzyme is involved in biosynthesis of D-mycaminose. It is synthesized by the Gram-positive bacterium Streptomyces fradiae as a dTDP-linked sugar
physiological function
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enzyme TylM1 is a dimethyltransferase from Streptomyces fradiae involved in the production of dTDP-mycaminose
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2 S-adenosyl-L-methionine + dTDP-3-amino-3,4,6-trideoxy-alpha-xylo-hexopyranose
2 S-adenosyl-L-homocysteine + dTDP-3-dimethylamino-3,4,6-trideoxy-alpha-xylo-hexopyranose
kcat/KM is about 3fold lower than kcat/Km for the natural substrated TDP-3-amino-3,6-dideoxy-alpha-D-glucopyranose
i.e. TDP-alpha-D-desosamine
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2 S-adenosyl-L-methionine + dTDP-3-amino-3,6-dideoxy-alpha-D-glucopyranose
2 S-adenosyl-L-homocysteine + dTDP-3-dimethylamino-3,6-dideoxy-alpha-D-glucopyranose
S-adenosyl-L-methionine + dTDP-3-methylamino-3,6-dideoxy-alpha-D-glucopyranose
S-adenosyl-L-homocysteine + dTDP-3-dimethylamino-3,6-dideoxy-alpha-D-glucopyranose
chemically prepared monomethylated compound is a substrate for TylM1 and could be swiftly converted by TylM1 to the dimethylated product. TylM1 catalyzes an N,N-dimethylation reaction by way of a monomethylated intermediate. Since the monomethylated amino group is intrinsically a better nucleophile than the unsubstituted amino group, the reaction rate of this SN2-type methyl transfer reaction is expected to be higher for the second half reaction than for the first methylation reaction
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additional information
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2 S-adenosyl-L-methionine + dTDP-3-amino-3,6-dideoxy-alpha-D-glucopyranose
2 S-adenosyl-L-homocysteine + dTDP-3-dimethylamino-3,6-dideoxy-alpha-D-glucopyranose
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2 S-adenosyl-L-methionine + dTDP-3-amino-3,6-dideoxy-alpha-D-glucopyranose
2 S-adenosyl-L-homocysteine + dTDP-3-dimethylamino-3,6-dideoxy-alpha-D-glucopyranose
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the enzyme is involved in biosynthesis of D-mycaminose. It is synthesized by the Gram-positive bacterium Streptomyces fradiae as a dTDP-linked sugar
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2 S-adenosyl-L-methionine + dTDP-3-amino-3,6-dideoxy-alpha-D-glucopyranose
2 S-adenosyl-L-homocysteine + dTDP-3-dimethylamino-3,6-dideoxy-alpha-D-glucopyranose
the enzyme is involved in the biosynthesis of mycaminose, an essential structural component of the macrolide antibiotic tylosin poduced by Streptomyces fradiae
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2 S-adenosyl-L-methionine + dTDP-3-amino-3,6-dideoxy-alpha-D-glucopyranose
2 S-adenosyl-L-homocysteine + dTDP-3-dimethylamino-3,6-dideoxy-alpha-D-glucopyranose
TylM1 has relaxed specificity toward its sugar substrate. The kcat/KM for dTDP-3-amino-4,6-dideoxy-alpha-D-glucopyranose is about 3fold lower than kcat/Km for the natural substrated TDP-3-amino-3,6-dideoxy-alpha-D-glucopyranose
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2 S-adenosyl-L-methionine + dTDP-3-amino-3,6-dideoxy-alpha-D-glucopyranose
2 S-adenosyl-L-homocysteine + dTDP-3-dimethylamino-3,6-dideoxy-alpha-D-glucopyranose
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i.e dTDP-mycaminose, binding pocket structure and binding mechanism, overview
analysis of the binding structure of the dTDP-sugar in enzyme TylM1 active site, overview. Only a water molecule is expelled from the active site to accommodate one of the methyl substituents on the C-3' amino group
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additional information
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the enzyme also catalyzes the methylation of dTDP-3-amino-3,6-dideoxy-alpha-D-galactopyranose, EC 2.1.1.236
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additional information
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modeling of substrate binding
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2 S-adenosyl-L-methionine + dTDP-3-amino-3,6-dideoxy-alpha-D-glucopyranose
2 S-adenosyl-L-homocysteine + dTDP-3-dimethylamino-3,6-dideoxy-alpha-D-glucopyranose
additional information
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the enzyme also catalyzes the methylation of dTDP-3-amino-3,6-dideoxy-alpha-D-galactopyranose, EC 2.1.1.236
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2 S-adenosyl-L-methionine + dTDP-3-amino-3,6-dideoxy-alpha-D-glucopyranose
2 S-adenosyl-L-homocysteine + dTDP-3-dimethylamino-3,6-dideoxy-alpha-D-glucopyranose
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2 S-adenosyl-L-methionine + dTDP-3-amino-3,6-dideoxy-alpha-D-glucopyranose
2 S-adenosyl-L-homocysteine + dTDP-3-dimethylamino-3,6-dideoxy-alpha-D-glucopyranose
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the enzyme is involved in biosynthesis of D-mycaminose. It is synthesized by the Gram-positive bacterium Streptomyces fradiae as a dTDP-linked sugar
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2 S-adenosyl-L-methionine + dTDP-3-amino-3,6-dideoxy-alpha-D-glucopyranose
2 S-adenosyl-L-homocysteine + dTDP-3-dimethylamino-3,6-dideoxy-alpha-D-glucopyranose
P95748
the enzyme is involved in the biosynthesis of mycaminose, an essential structural component of the macrolide antibiotic tylosin poduced by Streptomyces fradiae
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S-adenosyl-L-methionine
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additional information
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TylM1 is not a Mg2+-dependent methyltransferase
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0.045 - 0.93
dTDP-3-amino-3,6-dideoxy-alpha-D-glucopyranose
0.0468
dTDP-3-methylamino-3,6-dideoxy-alpha-D-glucopyranose
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pH 7.5, 24°C
0.0989 - 0.117
S-adenosyl-L-methionine
0.045
dTDP-3-amino-3,6-dideoxy-alpha-D-glucopyranose
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pH 8.5, 37°C, wild-type enzyme
0.0594
dTDP-3-amino-3,6-dideoxy-alpha-D-glucopyranose
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pH 7.5, 24°C
0.079
dTDP-3-amino-3,6-dideoxy-alpha-D-glucopyranose
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pH and temperature not specified in the publication
0.1184
dTDP-3-amino-3,6-dideoxy-alpha-D-glucopyranose
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pH 7.5, 24°C
0.67
dTDP-3-amino-3,6-dideoxy-alpha-D-glucopyranose
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pH 8.5, 37°C, mutant enzyme H123A
0.93
dTDP-3-amino-3,6-dideoxy-alpha-D-glucopyranose
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pH 8.5, 37°C, mutant enzyme H123N
0.0989
S-adenosyl-L-methionine
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pH 7.5, 24°C, cosubstrate: 1.28 mM dTDP-3-amino-3,6-dideoxy-alpha-D-glucopyranose
0.117
S-adenosyl-L-methionine
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pH 7.5, 24°C, cosubstrate: dTDP-3-methylamino-3,6-dideoxy-alpha-D-glucopyranose
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0.0126 - 0.75
dTDP-3-amino-3,6-dideoxy-alpha-D-glucopyranose
0.54
dTDP-3-methylamino-3,6-dideoxy-alpha-D-glucopyranose
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pH 7.5, 24°C
0.09 - 0.86
S-adenosyl-L-methionine
0.0126
dTDP-3-amino-3,6-dideoxy-alpha-D-glucopyranose
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pH 8.5, 37°C, mutant enzyme H123N
0.046
dTDP-3-amino-3,6-dideoxy-alpha-D-glucopyranose
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pH 8.5, 37°C, mutant enzyme H123A
0.12
dTDP-3-amino-3,6-dideoxy-alpha-D-glucopyranose
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pH 7.5, 24°C
0.165
dTDP-3-amino-3,6-dideoxy-alpha-D-glucopyranose
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pH 7.5, 24°C
0.172
dTDP-3-amino-3,6-dideoxy-alpha-D-glucopyranose
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pH 8.5, 37°C, wild-type enzyme
0.75
dTDP-3-amino-3,6-dideoxy-alpha-D-glucopyranose
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pH and temperature not specified in the publication
0.09
S-adenosyl-L-methionine
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pH 7.5, 24°C, cosubstrate: 1.28 mM dTDP-3-amino-3,6-dideoxy-alpha-D-glucopyranose
0.86
S-adenosyl-L-methionine
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pH 7.5, 24°C, cosubstrate: 0.89 mM dTDP-3-methylamino-3,6-dideoxy-alpha-D-glucopyranose
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0.0135 - 3.8
dTDP-3-amino-3,6-dideoxy-alpha-D-glucopyranose
11.5
dTDP-3-methylamino-3,6-dideoxy-alpha-D-glucopyranose
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pH 7.5, 24°C
0.91 - 7.35
S-adenosyl-L-methionine
0.0135
dTDP-3-amino-3,6-dideoxy-alpha-D-glucopyranose
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pH 8.5, 37°C, mutant enzyme H123N
0.069
dTDP-3-amino-3,6-dideoxy-alpha-D-glucopyranose
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pH 8.5, 37°C, mutant enzyme H123A
1
dTDP-3-amino-3,6-dideoxy-alpha-D-glucopyranose
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pH 7.5, 24°C
2.78
dTDP-3-amino-3,6-dideoxy-alpha-D-glucopyranose
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pH 7.5, 24°C
3.8
dTDP-3-amino-3,6-dideoxy-alpha-D-glucopyranose
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pH 8.5, 37°C, wild-type enzyme
0.91
S-adenosyl-L-methionine
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pH 7.5, 24°C, cosubstrate: 1.28 mM dTDP-3-amino-3,6-dideoxy-alpha-D-glucopyranose
7.35
S-adenosyl-L-methionine
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pH 7.5, 24°C, cosubstrate: dTDP-3-methylamino-3,6-dideoxy-alpha-D-glucopyranose
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27000
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2 * 27000, SDS-PAGE
27427
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2 * 27427, calculated from sequence
27530
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x * 27530, calculated from sequence
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x * 27530, calculated from sequence
homodimer
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2 * 27000, SDS-PAGE; 2 * 27427, calculated from sequence
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enzyme in complex with S-adenosyl-L-homocysteine and dTDP-3-N-methylamino-3,6-dideoxyglucose., X-ray diffraction structure determination and analysis at 1.6 A resolution
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hanging drop method of vapor diffusion method, high resolution X-ray structures of TylM1, one in which the enzyme contains bound SAM and dTDP-phenol and the second in which the protein is complexed with S-adenosyl-L-homocysteine and dTDP-3-amino-3,6-dideoxyglucose, its natural substrate. Combined, these two structures, solved to 1.35 A and 1.79 A resolution, respectively, show the orientations of SAM and the dTDP-linked sugar substrate within the active site region. Specifically, the C-30 amino group of the hexose is in the correct position for an in-line attack at the reactive methyl group of S-adenosyl-L-methionine. High-resolution X-ray models show that the observed perturbations in the kinetic constants of the mutant enzynes H123A and H123N are not due to major changes in their threedimensional folds. Most likely the proton on the C-3' amino group is transferred to one of the water molecules lining the active site pocket as catalysis proceeds
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concentrated TylM1 protein is stable and can endure repeated freeze/thaw cycles without losing noticeable activity
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inclusion of 0.1 mM S-adenosyl-L-methioninet in buffers is crucial to prevent TylM1 from precipitating during the purification
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TylM1 is unstable at low concentrations, requiring the addition of bovine serum albumin (1 mg/mL) to the assay buffer during kinetic studies of the
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-80 °C concentrated TylM1 protein is stable for at least 2 years
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inclusion of 0.1 mM AdoMet in buffers is crucial to prevent TylM1 from precipitating during the purification
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expression in Escherichia coli
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expression in Escherichia coli. Heterologous expression of the tylM1 gene in the desVI deletion mutant of Streptomyces venezuelae. TylM1 is a competent substitute for DesVI
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H123A
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mutant protein retains catalytic activity, the kcat/Km is reduced to 1.8% compared to the wild-type enzyme
H123N
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mutant protein retains catalytic activity, the kcat/Km is reduced to 0.37% compared to the wild-type enzyme
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medicine
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the enzyme is involved in biosynthesis of D-mycaminose. D-Mycaminose is an unusual dideoxy sugar found attached to the antibiotic tylosin, a commonly used veterinarian therapeutic
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TYLM1_STRFR
255
27428
Swiss-Prot
A0A0B5QC68_CLOBE
245
29130
TrEMBL
A0A117EC10_STRSC
249
27147
TrEMBL
A0A0J1IA23_9FIRM
247
27929
TrEMBL
A0A2K8RH71_9ACTN
267
29567
TrEMBL
A0A1S8TA52_9CLOT
245
29026
TrEMBL
A0A1Y6B233_BACCE
174
20059
TrEMBL
A0A1S8MYK5_CLOSA
245
28995
TrEMBL
A0A0K6MYY1_BACIU
179
20546
TrEMBL
A0A1S8T278_CLOBE
245
29170
TrEMBL
A0A1V5I1T2_9SPIR
250
28416
TrEMBL
A0A1S8P6C6_CLOBE
245
29143
TrEMBL
A0A2S2JL45_9LACO
243
28684
TrEMBL
A0A1E3GYF4_9RHIZ
201
22153
TrEMBL
A0A2S9YSR8_9DELT
204
22726
TrEMBL
A0A1V6EMT2_9BACT
243
26618
TrEMBL
A0A1V6DAB2_9CHLR
260
29749
TrEMBL
A0A1W7AC85_9STAP
238
27693
TrEMBL
A0A1S8SQF3_9CLOT
245
29154
TrEMBL
A0A0K6J6R2_BACCE
237
27358
TrEMBL
A0A161XEF4_9CELL
249
27519
TrEMBL
A0A2S0XF24_9RHIZ
211
22300
TrEMBL
A0A1V5Z9X1_9BACT
270
30811
TrEMBL
A0A1Y6IP85_9VIBR
201
22618
TrEMBL
A0A2T0BDK1_9CLOT
253
29800
TrEMBL
A0A0K0Y2S6_9RHOB
242
26659
TrEMBL
A0A1S6IMN9_9LACT
244
28242
TrEMBL
A0A1Y6AR95_BACCE
237
27463
TrEMBL
A0A2H5Y5Z3_9BACT
252
28966
TrEMBL
A0A1D8AYJ6_9BACT
223
24374
TrEMBL
A0A1V5QBT9_9BACT
259
29574
TrEMBL
A0A1V5Q5R9_9BACT
254
28428
TrEMBL
A0A1Y6AE47_BACCE
237
27583
TrEMBL
A0A2H6H3S2_9BACT
238
26419
TrEMBL
A0A2M9N1U3_9BACL
233
27231
TrEMBL
A0A0S4IF52_9PSED
203
22765
TrEMBL
A0A136KGI2_9BACT
248
28472
TrEMBL
A0A1V6F4H5_9BACT
272
31299
TrEMBL
A0A238KJA4_9RHOB
200
22114
TrEMBL
A0A1V5QYA2_9PROT
250
28324
TrEMBL
A0A1E7XC99_9LACO
251
29282
TrEMBL
A0A0Q9YJ38_9COXI
195
22471
TrEMBL
A0A2G4AWJ4_VIBSP
255
28913
TrEMBL
A0A2J7VMU0_9BURK
235
26860
TrEMBL
A0A2S9Y068_9BACI
237
27318
TrEMBL
A0A1S8PY40_CLOBE
245
29102
TrEMBL
A0A140L236_9CLOT
257
30414
TrEMBL
A0A136NZW0_9CHLR
245
27317
TrEMBL
A0A1S8SK59_CLOBE
245
29157
TrEMBL
A0A1Y5RD77_9RHOB
206
22580
TrEMBL
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Chen, H.; Yamase, H.; Murakami, K.; Chang, C.W.; Zhao, L.; Zhao, Z.; Liu, H.W.
Expression, purification, and characterization of two N,N-dimethyltransferases, tylM1 and desVI, involved in the biosynthesis of mycaminose and desosamine
Biochemistry
41
9165-9183
2002
Streptomyces fradiae (P95748)
brenda
Carney, A.E.; Holden, H.M.
Molecular architecture of TylM1 from Streptomyces fradiae: an N,N-dimethyltransferase involved in the production of dTDP-D-mycaminose
Biochemistry
50
780-787
2011
Streptomyces fradiae (P95748), Streptomyces fradiae
brenda
Gandecha, A.R.; Large, S.L.; Cundliffe, E.
Analysis of four tylosin biosynthetic genes from the tylLM region of the Streptomyces fradiae genome
Gene
184
197-203
1997
Streptomyces fradiae (P95748)
brenda
Thoden, J.B.; Holden, H.M.
Production of a novel N-monomethylated dideoxysugar
Biochemistry
53
1105-1107
2014
Streptomyces fradiae (P95748), Streptomyces fradiae
brenda
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