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Information on EC 2.1.1.236 - dTDP-3-amino-3,6-dideoxy-alpha-D-galactopyranose N,N-dimethyltransferase and Organism(s) Streptomyces fradiae and UniProt Accession P95748

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IUBMB Comments
The enzyme is involved in the synthesis of dTDP-D-ravidosamine, the amino sugar moiety of the antibiotic ravidomycin V, which is produced by the bacterium Streptomyces ravidus.
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This record set is specific for:
Streptomyces fradiae
UNIPROT: P95748
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The taxonomic range for the selected organisms is: Streptomyces fradiae
The expected taxonomic range for this enzyme is: Streptomyces
Synonyms
ravnmt, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SYSTEMATIC NAME
IUBMB Comments
S-adenosyl-L-methionine:dTDP-3-amino-3,6-dideoxy-alpha-D-galactopyranose 3-N,N-dimethyltransferase
The enzyme is involved in the synthesis of dTDP-D-ravidosamine, the amino sugar moiety of the antibiotic ravidomycin V, which is produced by the bacterium Streptomyces ravidus.
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
2 S-adenosyl-L-methionine + dTDP-3-amino-3,6-dideoxy-alpha-D-galactopyranose
2 S-adenosyl-L-homocysteine + dTDP-3-dimethylamino-3,6-dideoxy-alpha-D-galactopyranose
show the reaction diagram
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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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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
2 S-adenosyl-L-methionine + dTDP-3-amino-3,6-dideoxy-alpha-D-galactopyranose
2 S-adenosyl-L-homocysteine + dTDP-3-dimethylamino-3,6-dideoxy-alpha-D-galactopyranose
show the reaction diagram
-
-
-
?
additional information
?
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the enzyme also catalyzes the methylation of dTDP-3-amino-3,6-dideoxy-alpha-D-glucopyranose, EC 2.1.1.235
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-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
S-adenosyl-L-methionine
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1.54
dTDP-3-amino-3,6-dideoxy-alpha-D-galactopyranose
pH and temperature not specified in the publication
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.61
dTDP-3-amino-3,6-dideoxy-alpha-D-galactopyranose
pH and temperature not specified in the publication
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
enzyme TylM1 is a dimethyltransferase from Streptomyces fradiae involved in the production of dTDP-mycaminose
additional information
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
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
TYLM1_STRFR
255
0
27428
Swiss-Prot
-
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
enzyme in complex with S-adenosyl-L-homocysteine and dTDP-3-N-methylamino-3,6-dideoxygalactose., X-ray diffraction structure determination and analysis at 2.2 A resolution
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Thoden, J.B.; Holden, H.M.
Production of a novel N-monomethylated dideoxysugar
Biochemistry
53
1105-1107
2014
Streptomyces fradiae (P95748)
Manually annotated by BRENDA team