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Literature summary for 2.3.1.136 extracted from

  • Lee, H.J.; Rakic, B.; Gilbert, M.; Wakarchuk, W.W.; Withers, S.G.; Strynadka, N.C.
    Structural and kinetic characterizations of the polysialic acid O-acetyltransferase OatWY from Neisseria meningitidis (2009), J. Biol. Chem., 284, 24501-24511.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

Cloned (Comment) Organism
expressed in Escherichia coli as a His-tagged fusion protein Neisseria meningitidis

Crystallization (Commentary)

Crystallization (Comment) Organism
OatWY is crystalised with bound substrate acetyl-CoA and its analogs (CoA, S-(2-oxopropyl)-CoA) using the hanging drop vapor diffusion technique. The structure of OatWY reveals an intimate homotrimer of left-handed beta-helix motifs that frame a deep active site cleft selective for the polysialic acid-bearing substrate. A significant movement of Tyr-171 blocks the active site of the enzyme in its native form Neisseria meningitidis

Protein Variants

Protein Variants Comment Organism
H121A mutant shows dramatically reduced activity Neisseria meningitidis
W145A mutant shows dramatically reduced activity Neisseria meningitidis
Y171A mutant shows dramatically reduced activity Neisseria meningitidis

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.011
-
([Glc-(alpha1-4)-Sia]n)
-
Neisseria meningitidis
0.21
-
acetyl-CoA
-
Neisseria meningitidis

Organism

Organism UniProt Comment Textmining
Neisseria meningitidis O33391
-
-

Purification (Commentary)

Purification (Comment) Organism
using affnitiy chromatography and ion-exchange chromatography Neisseria meningitidis

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
acetyl-CoA + ([Glc-(alpha1-4)-Sia]) relative activity: 19.2% Neisseria meningitidis ?
-
?
acetyl-CoA + ([Glc-(alpha1-4)-Sia]n) relative activity: 100% Neisseria meningitidis ?
-
?
acetyl-CoA + colominic acid relative activity: 2.1% Neisseria meningitidis ?
-
?
additional information when S-(2-oxopropyl)-CoA is used as a donor activity is dramatically reduced Neisseria meningitidis ?
-
?

Subunits

Subunits Comment Organism
homotrimer crystal structure Neisseria meningitidis

Synonyms

Synonyms Comment Organism
OatWY
-
Neisseria meningitidis
polysialic-acid O-acetyltransferase
-
Neisseria meningitidis

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
25
-
assay at Neisseria meningitidis

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
1.3
-
acetyl-CoA
-
Neisseria meningitidis
2.1
-
([Glc-(alpha1-4)-Sia]n)
-
Neisseria meningitidis

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.5
-
assay at Neisseria meningitidis

kcat/KM [mM/s]

kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
6.3
-
acetyl-CoA
-
Neisseria meningitidis
190
-
([-6)-Glc-(alpha1-4)-Sia-(alpha2-]n) oder ([-6)-Glc-(alpha1-4)-Sia-(alpha2-]n)
-
Neisseria meningitidis