Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary for 2.4.1.322 extracted from

  • Mulichak, A.M.; Lu, W.; Losey, H.C.; Walsh, C.T.; Garavito, R.M.
    Crystal structure of vancosaminyltransferase GtfD from the vancomycin biosynthetic pathway: interactions with acceptor and nucleotide ligands (2004), Biochemistry, 43, 5170-5180.
    View publication on PubMed
Search for more literature for 2.4.1.322

Cloned(Commentary)

Cloned (Comment) Organism
-
 Amycolatopsis orientalis

Crystallization (Commentary)

Crystallization (Comment) Organism
hanging drop vapor diffusion method, X-ray crystal structure of GtfD as a complex with TDP and desvancosaminyl-vancomycin at 2.0 A resolution Amycolatopsis orientalis

Protein Variants

Protein Variants Comment Organism
D13A 5630fold decrease in kcat for UDP-L-epi-vancosamine Amycolatopsis orientalis
T10A 172fold decrease in kcat/Km for UDP-L-epi-vancosamine Amycolatopsis orientalis

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.016
-
 desvancosaminyl-vancomycin pH 7.0, 37°C, wild-type enzyme Amycolatopsis orientalis
0.027
-
 desvancosaminyl-vancomycin pH 7.0, 37°C, mutant enzyme T10A Amycolatopsis orientalis
2
-
 UDP-L-epi-vancosamine pH 7.0, 37°C, wild-type enzyme Amycolatopsis orientalis

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
42881
-
 x * 42881, calculation from sequence Amycolatopsis orientalis

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
dTDP-beta-L-vancosamine + devancosaminyl-vancomycin Amycolatopsis orientalis the enzyme catalyses the ultimate step in the biosynthesis of the antibiotic vancomycin dTDP + vancomycin
-
 ?

Organism

Organism UniProt Comment Textmining
Amycolatopsis orientalis Q9AFC7
-
-

Purification (Commentary)

Purification (Comment) Organism
-
 Amycolatopsis orientalis

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
dTDP-beta-L-vancosamine + devancosaminyl-vancomycin the enzyme catalyses the ultimate step in the biosynthesis of the antibiotic vancomycin Amycolatopsis orientalis dTDP + vancomycin
-
 ?
dTDP-beta-L-vancosamine + devancosaminyl-vancomycin dTDP-beta-L-vancosamine i.e. dTDP-3-amino-2,3,6-trideoxy-3-C-methyl-beta-L-lyxo-hexopyranose. The enzyme binds TDP in the interdomain cleft, while the aglycone acceptor binds in a deep crevice in the N-terminal domain. The two domains are interdependent in terms of substrate binding and overall structure. Asp13 is a catalytic general base, with a possible secondary role for Thr10 Amycolatopsis orientalis dTDP + vancomycin
-
 ?
UDP-L-epi-vancosamine + devancosaminyl-vancomycin
-
 Amycolatopsis orientalis UDP + ?
-
 ?

Subunits

Subunits Comment Organism
? x * 42881, calculation from sequence Amycolatopsis orientalis

Synonyms

Synonyms Comment Organism
desvancosamine-vancomycin TDP-vancosaminyltransferase
-
 Amycolatopsis orientalis
GtfD
-
 Amycolatopsis orientalis

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
37
-
 assay at Amycolatopsis orientalis

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
0.002
-
 desvancosaminyl-vancomycin pH 7.0, 37°C, mutant enzyme D13A Amycolatopsis orientalis
0.002
-
 UDP-L-epi-vancosamine pH 7.0, 37°C, mutant enzyme D13A Amycolatopsis orientalis
1.12
-
 desvancosaminyl-vancomycin pH 7.0, 37°C, wild-type enzyme Amycolatopsis orientalis
1.12
-
 UDP-L-epi-vancosamine pH 7.0, 37°C, wild-type enzyme Amycolatopsis orientalis

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7
-
 assay at Amycolatopsis orientalis

kcat/KM [mM/s]

kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
0.0033
-
 UDP-L-epi-vancosamine pH 7.0, 37°C, mutant enzyme T10A Amycolatopsis orientalis
0.56
-
 UDP-L-epi-vancosamine pH 7.0, 37°C, wild-type enzyme Amycolatopsis orientalis