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Literature summary for 2.4.1.264 extracted from

  • Barreras, M.; Salinas, S.R.; Abdian, P.L.; Kampel, M.A.; Ielpi, L.
    Structure and mechanism of GumK, a membrane-associated glucuronosyltransferase (2008), J. Biol. Chem., 283, 25027-25035.
    View publication on PubMedView publication on EuropePMC

Crystallization (Commentary)

Crystallization (Comment) Organism
hanging drop vapour diffusion method, crystal structure of apo-enzyme at 1.9 A resolution, and of enzyme in complex with UDP, at 2.28 A resolution. Residue Asp157 serves as the general base in the transfer reaction. Residues M231, M273, E272, Y292, M306, K307, and Q310 interact with UDP. Cocrystallisation of GumK or mutant D157A in presence of UDP-glucuronate is not possible Xanthomonas campestris

Protein Variants

Protein Variants Comment Organism
D157A mutation in UDP binding site, loss of activity Xanthomonas campestris
D157E mutation in UDP binding site, loss of activity Xanthomonas campestris
D157N mutation in UDP binding site, loss of activity Xanthomonas campestris
D207A mutation in UDP binding site, kcat/Km for UDP-glucuronate is identical to wild-type value Xanthomonas campestris
D234A mutation in UDP binding site, kcat/Km for UDP-glucuronate is identical to wild-type value Xanthomonas campestris
E192A mutation in UDP binding site, kcat/Km for UDP-glucuronate is identical to wild-type value Xanthomonas campestris
E272A mutation in UDP binding site, kcat/KM is 4.6fold lower than wild-type value Xanthomonas campestris
E272D mutation in UDP binding site, kcat/KM is 2fold lower than wild-type value Xanthomonas campestris
K307A mutation in UDP binding site, kcat/KM is 560fold lower than wild-type value Xanthomonas campestris
M231A mutation in UDP binding site, kcat/Km for UDP-glucuronate is similar to wild-type value Xanthomonas campestris
Q310A mutation in UDP binding site, kcat/KM is 22.2fold lower than wild-type value Xanthomonas campestris
Y292A mutation in UDP binding site, kcat/KM is 14.7fold lower than wild-type value Xanthomonas campestris

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.06
-
UDP-glucuronate mutant D207A, pH 8.2, 20°C Xanthomonas campestris
0.061
-
UDP-glucuronate mutant E192A, pH 8.2, 20°C Xanthomonas campestris
0.062
-
UDP-glucuronate wild-type, pH 8.2, 20°C Xanthomonas campestris
0.063
-
UDP-glucuronate mutant D234A, pH 8.2, 20°C Xanthomonas campestris
0.063
-
UDP-glucuronate mutant M231A, pH 8.2, 20°C Xanthomonas campestris
0.1
-
UDP-glucuronate mutant E272D, pH 8.2, 20°C Xanthomonas campestris
0.125
-
UDP-glucuronate mutant E272A, pH 8.2, 20°C Xanthomonas campestris
0.194
-
D-Man-alpha-(1->3)-D-Glc-beta-(1->4)-D-Glc-alpha-1-diphosphopolyisoprenol mutant D207A, pH 8.2, 20°C Xanthomonas campestris
0.198
-
D-Man-alpha-(1->3)-D-Glc-beta-(1->4)-D-Glc-alpha-1-diphosphopolyisoprenol wild-type, pH 8.2, 20°C Xanthomonas campestris
0.199
-
D-Man-alpha-(1->3)-D-Glc-beta-(1->4)-D-Glc-alpha-1-diphosphopolyisoprenol mutant E192A, pH 8.2, 20°C Xanthomonas campestris
0.205
-
D-Man-alpha-(1->3)-D-Glc-beta-(1->4)-D-Glc-alpha-1-diphosphopolyisoprenol mutant D234A, pH 8.2, 20°C Xanthomonas campestris
0.21
-
UDP-glucuronate mutant Y292A, pH 8.2, 20°C Xanthomonas campestris
0.218
-
D-Man-alpha-(1->3)-D-Glc-beta-(1->4)-D-Glc-alpha-1-diphosphopolyisoprenol mutant M231A, pH 8.2, 20°C Xanthomonas campestris
0.246
-
D-Man-alpha-(1->3)-D-Glc-beta-(1->4)-D-Glc-alpha-1-diphosphopolyisoprenol mutant Q310A, pH 8.2, 20°C Xanthomonas campestris
0.267
-
D-Man-alpha-(1->3)-D-Glc-beta-(1->4)-D-Glc-alpha-1-diphosphopolyisoprenol mutant E272D, pH 8.2, 20°C Xanthomonas campestris
0.274
-
D-Man-alpha-(1->3)-D-Glc-beta-(1->4)-D-Glc-alpha-1-diphosphopolyisoprenol mutant Y292A, pH 8.2, 20°C Xanthomonas campestris
0.291
-
D-Man-alpha-(1->3)-D-Glc-beta-(1->4)-D-Glc-alpha-1-diphosphopolyisoprenol mutant E272A, pH 8.2, 20°C Xanthomonas campestris
0.39
-
D-Man-alpha-(1->3)-D-Glc-beta-(1->4)-D-Glc-alpha-1-diphosphopolyisoprenol mutant K307A, pH 8.2, 20°C Xanthomonas campestris
0.44
-
UDP-glucuronate mutant K307A, pH 8.2, 20°C Xanthomonas campestris
1.19
-
UDP-glucuronate mutant Q310A, pH 8.2, 20°C Xanthomonas campestris

Localization

Localization Comment Organism GeneOntology No. Textmining
membrane
-
Xanthomonas campestris 16020
-

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
UDP-glucuronate + D-Man-alpha-(1->3)-D-Glc-beta-(1->4)-D-Glc-alpha-1-diphosphopolyisoprenol Xanthomonas campestris the enzyme is involved in biosynthesis of xanthan UDP + GlcA-beta-(1->2)-D-Man-alpha-(1->3)-D-Glc-beta-(1->4)-D-Glc-alpha-1-diphosphopolyisoprenol
-
?

Organism

Organism UniProt Comment Textmining
Xanthomonas campestris Q8GCH2
-
-

Purification (Commentary)

Purification (Comment) Organism
-
Xanthomonas campestris

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
UDP-glucuronate + D-Man-alpha-(1->3)-D-Glc-beta-(1->4)-D-Glc-alpha-1-diphosphopolyisoprenol
-
Xanthomonas campestris UDP + GlcA-beta-(1->2)-D-Man-alpha-(1->3)-D-Glc-beta-(1->4)-D-Glc-alpha-1-diphosphopolyisoprenol
-
?
UDP-glucuronate + D-Man-alpha-(1->3)-D-Glc-beta-(1->4)-D-Glc-alpha-1-diphosphopolyisoprenol the enzyme is involved in biosynthesis of xanthan Xanthomonas campestris UDP + GlcA-beta-(1->2)-D-Man-alpha-(1->3)-D-Glc-beta-(1->4)-D-Glc-alpha-1-diphosphopolyisoprenol
-
?

Synonyms

Synonyms Comment Organism
gumK
-
Xanthomonas campestris

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
0.0011
-
UDP-glucuronate mutant K307A, pH 8.2, 20°C Xanthomonas campestris
0.02
-
UDP-glucuronate mutant Y292A, pH 8.2, 20°C Xanthomonas campestris
0.038
-
UDP-glucuronate mutant E272A, pH 8.2, 20°C Xanthomonas campestris
0.072
-
UDP-glucuronate mutant E272D, pH 8.2, 20°C Xanthomonas campestris
0.075
-
UDP-glucuronate mutant Q310A, pH 8.2, 20°C Xanthomonas campestris
0.084
-
UDP-glucuronate mutant D207A, pH 8.2, 20°C Xanthomonas campestris
0.087
-
UDP-glucuronate mutant E192A, pH 8.2, 20°C Xanthomonas campestris
0.087
-
UDP-glucuronate mutant M231A, pH 8.2, 20°C Xanthomonas campestris
0.087
-
UDP-glucuronate wild-type, pH 8.2, 20°C Xanthomonas campestris
0.088
-
UDP-glucuronate mutant D234A, pH 8.2, 20°C Xanthomonas campestris

General Information

General Information Comment Organism
physiological function the enzyme is involved in biosynthesis of xanthan Xanthomonas campestris

kcat/KM [mM/s]

kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
0.0025
-
UDP-glucuronate mutant K307A, pH 8.2, 20°C Xanthomonas campestris
0.063
-
UDP-glucuronate mutant Q310A, pH 8.2, 20°C Xanthomonas campestris
0.095
-
UDP-glucuronate mutant Y292A, pH 8.2, 20°C Xanthomonas campestris
0.304
-
UDP-glucuronate mutant E272A, pH 8.2, 20°C Xanthomonas campestris
0.72
-
UDP-glucuronate mutant E272D, pH 8.2, 20°C Xanthomonas campestris
1.28
-
UDP-glucuronate mutant M231A, pH 8.2, 20°C Xanthomonas campestris
1.4
-
UDP-glucuronate mutant D207A, pH 8.2, 20°C Xanthomonas campestris
1.4
-
UDP-glucuronate mutant D234A, pH 8.2, 20°C Xanthomonas campestris
1.4
-
UDP-glucuronate wild-type, pH 8.2, 20°C Xanthomonas campestris
1.42
-
UDP-glucuronate mutant E192A, pH 8.2, 20°C Xanthomonas campestris