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Literature summary 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)

EC Number Crystallization (Comment) Organism
2.4.1.264 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

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

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
2.4.1.264 0.06
-
UDP-glucuronate mutant D207A, pH 8.2, 20°C Xanthomonas campestris
2.4.1.264 0.061
-
UDP-glucuronate mutant E192A, pH 8.2, 20°C Xanthomonas campestris
2.4.1.264 0.062
-
UDP-glucuronate wild-type, pH 8.2, 20°C Xanthomonas campestris
2.4.1.264 0.063
-
UDP-glucuronate mutant D234A, pH 8.2, 20°C Xanthomonas campestris
2.4.1.264 0.063
-
UDP-glucuronate mutant M231A, pH 8.2, 20°C Xanthomonas campestris
2.4.1.264 0.1
-
UDP-glucuronate mutant E272D, pH 8.2, 20°C Xanthomonas campestris
2.4.1.264 0.125
-
UDP-glucuronate mutant E272A, pH 8.2, 20°C Xanthomonas campestris
2.4.1.264 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
2.4.1.264 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
2.4.1.264 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
2.4.1.264 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
2.4.1.264 0.21
-
UDP-glucuronate mutant Y292A, pH 8.2, 20°C Xanthomonas campestris
2.4.1.264 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
2.4.1.264 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
2.4.1.264 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
2.4.1.264 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
2.4.1.264 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
2.4.1.264 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
2.4.1.264 0.44
-
UDP-glucuronate mutant K307A, pH 8.2, 20°C Xanthomonas campestris
2.4.1.264 1.19
-
UDP-glucuronate mutant Q310A, pH 8.2, 20°C Xanthomonas campestris

Localization

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

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
2.4.1.264 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

EC Number Organism UniProt Comment Textmining
2.4.1.264 Xanthomonas campestris Q8GCH2
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
2.4.1.264
-
Xanthomonas campestris

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.4.1.264 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
-
?
2.4.1.264 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

EC Number Synonyms Comment Organism
2.4.1.264 gumK
-
Xanthomonas campestris

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
2.4.1.264 0.0011
-
UDP-glucuronate mutant K307A, pH 8.2, 20°C Xanthomonas campestris
2.4.1.264 0.02
-
UDP-glucuronate mutant Y292A, pH 8.2, 20°C Xanthomonas campestris
2.4.1.264 0.038
-
UDP-glucuronate mutant E272A, pH 8.2, 20°C Xanthomonas campestris
2.4.1.264 0.072
-
UDP-glucuronate mutant E272D, pH 8.2, 20°C Xanthomonas campestris
2.4.1.264 0.075
-
UDP-glucuronate mutant Q310A, pH 8.2, 20°C Xanthomonas campestris
2.4.1.264 0.084
-
UDP-glucuronate mutant D207A, pH 8.2, 20°C Xanthomonas campestris
2.4.1.264 0.087
-
UDP-glucuronate mutant E192A, pH 8.2, 20°C Xanthomonas campestris
2.4.1.264 0.087
-
UDP-glucuronate mutant M231A, pH 8.2, 20°C Xanthomonas campestris
2.4.1.264 0.087
-
UDP-glucuronate wild-type, pH 8.2, 20°C Xanthomonas campestris
2.4.1.264 0.088
-
UDP-glucuronate mutant D234A, pH 8.2, 20°C Xanthomonas campestris

General Information

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

kcat/KM [mM/s]

EC Number kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
2.4.1.264 0.0025
-
UDP-glucuronate mutant K307A, pH 8.2, 20°C Xanthomonas campestris
2.4.1.264 0.063
-
UDP-glucuronate mutant Q310A, pH 8.2, 20°C Xanthomonas campestris
2.4.1.264 0.095
-
UDP-glucuronate mutant Y292A, pH 8.2, 20°C Xanthomonas campestris
2.4.1.264 0.304
-
UDP-glucuronate mutant E272A, pH 8.2, 20°C Xanthomonas campestris
2.4.1.264 0.72
-
UDP-glucuronate mutant E272D, pH 8.2, 20°C Xanthomonas campestris
2.4.1.264 1.28
-
UDP-glucuronate mutant M231A, pH 8.2, 20°C Xanthomonas campestris
2.4.1.264 1.4
-
UDP-glucuronate mutant D207A, pH 8.2, 20°C Xanthomonas campestris
2.4.1.264 1.4
-
UDP-glucuronate mutant D234A, pH 8.2, 20°C Xanthomonas campestris
2.4.1.264 1.4
-
UDP-glucuronate wild-type, pH 8.2, 20°C Xanthomonas campestris
2.4.1.264 1.42
-
UDP-glucuronate mutant E192A, pH 8.2, 20°C Xanthomonas campestris