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

BRENDA support

Literature summary for 5.4.99.9 extracted from

  • Tanner, J.J.; Boechi, L.; Andrew McCammon, J.; Sobrado, P.
    Structure, mechanism, and dynamics of UDP-galactopyranose mutase (2014), Arch. Biochem. Biophys., 544, 128-141.
    View publication on PubMedView publication on EuropePMC

Activating Compound

Activating Compound Comment Organism Structure
additional information enzyme activation mechanism, overview Trypanosoma cruzi
additional information enzyme activation mechanism, overview Aspergillus fumigatus
additional information enzme activation mechanism, overview Klebsiella pneumoniae
additional information enzme activation mechanism, overview Deinococcus radiodurans
NAD(P)H enzyme activation mechanism, overview Escherichia coli
NAD(P)H kinetic parameters for the reduction of eukaryotic UGMs by NAD(P)H, NAD(P)H site structure and conformational changes associated with enzyme activation, overview Trypanosoma cruzi
NAD(P)H kinetic parameters for the reduction of eukaryotic UGMs by NAD(P)H, NAD(P)H site structure and conformational changes associated with enzyme activation, overview Leishmania mexicana
NAD(P)H kinetic parameters for the reduction of eukaryotic UGMs by NAD(P)H, NAD(P)H site structure and conformational changes associated with enzyme activation, overview Aspergillus fumigatus
NAD(P)H kinetic parameters for the reduction of eukaryotic UGMs by NAD(P)H, NAD(P)H site structure and conformational changes associated with enzyme activation, overview Leishmania major
NAD(P)H kinetic parameters for the reduction of eukaryotic UGMs by NAD(P)H, NAD(P)H site structure and conformational changes associated with enzyme activation, overview Leishmania infantum

Crystallization (Commentary)

Crystallization (Comment) Organism
crystal structure analysis Escherichia coli
crystal structure analysis Klebsiella pneumoniae
crystal structure analysis Mycobacterium tuberculosis
crystal structure analysis Trypanosoma cruzi
crystal structure analysis Deinococcus radiodurans
crystal structure analysis, two crystal forms, hexagonal and triclinic Aspergillus fumigatus

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
UDP-alpha-D-galactopyranose Escherichia coli
-
UDP-alpha-D-galactofuranose
-
r
UDP-alpha-D-galactopyranose Klebsiella pneumoniae
-
UDP-alpha-D-galactofuranose
-
r
UDP-alpha-D-galactopyranose Mycobacterium tuberculosis
-
UDP-alpha-D-galactofuranose
-
r
UDP-alpha-D-galactopyranose Trypanosoma cruzi
-
UDP-alpha-D-galactofuranose
-
r
UDP-alpha-D-galactopyranose Leishmania mexicana
-
UDP-alpha-D-galactofuranose
-
r
UDP-alpha-D-galactopyranose Aspergillus fumigatus
-
UDP-alpha-D-galactofuranose
-
r
UDP-alpha-D-galactopyranose Leishmania major
-
UDP-alpha-D-galactofuranose
-
r
UDP-alpha-D-galactopyranose Leishmania infantum
-
UDP-alpha-D-galactofuranose
-
r
UDP-alpha-D-galactopyranose Deinococcus radiodurans
-
UDP-alpha-D-galactofuranose
-
r
UDP-alpha-D-galactopyranose Deinococcus radiodurans R1 / ATCC 13939 / DSM 20539
-
UDP-alpha-D-galactofuranose
-
r

Organism

Organism UniProt Comment Textmining
Aspergillus fumigatus
-
-
-
Deinococcus radiodurans
-
-
-
Deinococcus radiodurans R1 / ATCC 13939 / DSM 20539
-
-
-
Escherichia coli
-
-
-
Klebsiella pneumoniae
-
-
-
Leishmania infantum
-
-
-
Leishmania major
-
-
-
Leishmania mexicana
-
-
-
Mycobacterium tuberculosis
-
-
-
Trypanosoma cruzi
-
-
-

Reaction

Reaction Comment Organism Reaction ID
UDP-alpha-D-galactopyranose = UDP-alpha-D-galactofuranose chemical reaction mechanism, overview Escherichia coli
UDP-alpha-D-galactopyranose = UDP-alpha-D-galactofuranose chemical reaction mechanism, overview Klebsiella pneumoniae
UDP-alpha-D-galactopyranose = UDP-alpha-D-galactofuranose chemical reaction mechanism, overview Trypanosoma cruzi
UDP-alpha-D-galactopyranose = UDP-alpha-D-galactofuranose chemical reaction mechanism, overview Aspergillus fumigatus
UDP-alpha-D-galactopyranose = UDP-alpha-D-galactofuranose chemical reaction mechanism, overview Deinococcus radiodurans

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
UDP-alpha-D-galactopyranose
-
Escherichia coli UDP-alpha-D-galactofuranose
-
r
UDP-alpha-D-galactopyranose
-
Klebsiella pneumoniae UDP-alpha-D-galactofuranose
-
r
UDP-alpha-D-galactopyranose
-
Mycobacterium tuberculosis UDP-alpha-D-galactofuranose
-
r
UDP-alpha-D-galactopyranose
-
Trypanosoma cruzi UDP-alpha-D-galactofuranose
-
r
UDP-alpha-D-galactopyranose
-
Leishmania mexicana UDP-alpha-D-galactofuranose
-
r
UDP-alpha-D-galactopyranose
-
Aspergillus fumigatus UDP-alpha-D-galactofuranose
-
r
UDP-alpha-D-galactopyranose
-
Leishmania major UDP-alpha-D-galactofuranose
-
r
UDP-alpha-D-galactopyranose
-
Leishmania infantum UDP-alpha-D-galactofuranose
-
r
UDP-alpha-D-galactopyranose
-
Deinococcus radiodurans UDP-alpha-D-galactofuranose
-
r
UDP-alpha-D-galactopyranose the equilibrium of the UGM-catalyzed reaction favors UDP-Galp by the ratio of 11:1 Escherichia coli UDP-alpha-D-galactofuranose
-
r
UDP-alpha-D-galactopyranose the equilibrium of the UGM-catalyzed reaction favors UDP-Galp by the ratio of 11:1 Klebsiella pneumoniae UDP-alpha-D-galactofuranose
-
r
UDP-alpha-D-galactopyranose the equilibrium of the UGM-catalyzed reaction favors UDP-Galp by the ratio of 11:1 Mycobacterium tuberculosis UDP-alpha-D-galactofuranose
-
r
UDP-alpha-D-galactopyranose the equilibrium of the UGM-catalyzed reaction favors UDP-Galp by the ratio of 11:1 Trypanosoma cruzi UDP-alpha-D-galactofuranose
-
r
UDP-alpha-D-galactopyranose the equilibrium of the UGM-catalyzed reaction favors UDP-Galp by the ratio of 11:1 Leishmania mexicana UDP-alpha-D-galactofuranose
-
r
UDP-alpha-D-galactopyranose the equilibrium of the UGM-catalyzed reaction favors UDP-Galp by the ratio of 11:1 Aspergillus fumigatus UDP-alpha-D-galactofuranose
-
r
UDP-alpha-D-galactopyranose the equilibrium of the UGM-catalyzed reaction favors UDP-Galp by the ratio of 11:1 Leishmania major UDP-alpha-D-galactofuranose
-
r
UDP-alpha-D-galactopyranose the equilibrium of the UGM-catalyzed reaction favors UDP-Galp by the ratio of 11:1 Leishmania infantum UDP-alpha-D-galactofuranose
-
r
UDP-alpha-D-galactopyranose the equilibrium of the UGM-catalyzed reaction favors UDP-Galp by the ratio of 11:1 Deinococcus radiodurans UDP-alpha-D-galactofuranose
-
r
UDP-alpha-D-galactopyranose
-
Deinococcus radiodurans R1 / ATCC 13939 / DSM 20539 UDP-alpha-D-galactofuranose
-
r
UDP-alpha-D-galactopyranose the equilibrium of the UGM-catalyzed reaction favors UDP-Galp by the ratio of 11:1 Deinococcus radiodurans R1 / ATCC 13939 / DSM 20539 UDP-alpha-D-galactofuranose
-
r

Subunits

Subunits Comment Organism
decamer pentamer-of-dimers, in crystals Deinococcus radiodurans
dimer in solution Deinococcus radiodurans
dimer the dimer is a semicircular particle with the interface formed by domain 2 of one protomer packing against the beta-sheet of domain 3 of another protomer Escherichia coli
dimer the dimer is a semicircular particle with the interface formed by domain 2 of one protomer packing against the beta-sheet of domain 3 of another protomer Klebsiella pneumoniae
dimer the dimer is a semicircular particle with the interface formed by domain 2 of one protomer packing against the beta-sheet of domain 3 of another protomer Mycobacterium tuberculosis
monomer the unique fold-level variations exhibited by TcUGM are responsible for the monomeric state Trypanosoma cruzi
More oligomeric state and quaternary structure, overview Trypanosoma cruzi
More the tertiary structure dictates the oligomeric state, oligomeric state and quaternary structure, overview Aspergillus fumigatus
tetramer dimer-of-dimers tetramer in solution, the C-terminal helix of domain 1 and residue Arg133 in AfUGM form intersubunit hydrogen bonds in the AfUGM tetramer, while long side chains protruding from a helix of domain 2 likely prevent formation of the intersubunit 4-helix bundle that stabilizes the AfUGM tetramer Aspergillus fumigatus

Synonyms

Synonyms Comment Organism
UGM
-
Escherichia coli
UGM
-
Klebsiella pneumoniae
UGM
-
Mycobacterium tuberculosis
UGM
-
Trypanosoma cruzi
UGM
-
Leishmania mexicana
UGM
-
Aspergillus fumigatus
UGM
-
Leishmania major
UGM
-
Leishmania infantum
UGM
-
Deinococcus radiodurans

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7
-
assay at Escherichia coli
7
-
assay at Klebsiella pneumoniae
7
-
assay at Mycobacterium tuberculosis
7
-
assay at Trypanosoma cruzi
7
-
assay at Leishmania mexicana
7
-
assay at Aspergillus fumigatus
7
-
assay at Leishmania major
7
-
assay at Leishmania infantum
7
-
assay at Deinococcus radiodurans

Cofactor

Cofactor Comment Organism Structure
flavin flavoenzyme Klebsiella pneumoniae
flavin flavoenzyme Mycobacterium tuberculosis
flavin flavoenzyme Leishmania mexicana
flavin flavoenzyme Leishmania major
flavin flavoenzyme Leishmania infantum
flavin flavoenzyme Deinococcus radiodurans
flavin flavoenzyme, conformational changes induced by flavin reduction, overview Trypanosoma cruzi
flavin flavoenzyme, reduction of AfUGM also changes the conformation of the flavin itself, enzyme conformational changes induced by flavin reduction, overview Aspergillus fumigatus
flavin flavoenzyme, required for enzyme activation mechanism, overview Escherichia coli

General Information

General Information Comment Organism
evolution substrate recognition of bacterial and eukaryotic enzyme, involving a dynamic Arg, conserved steric interactions, and enzyme-substrate noncovalent interactions, overview. Domain 1 is important for positioning Galp for nucleophilic attack, domain 2 provides most of the interactions with the uridine group, and domain 3 figures prominently in binding the diphosphate Escherichia coli
evolution substrate recognition of bacterial and eukaryotic enzyme, involving a dynamic Arg, conserved steric interactions, and enzyme-substrate noncovalent interactions, overview. Domain 1 is important for positioning Galp for nucleophilic attack, domain 2 provides most of the interactions with the uridine group, and domain 3 figures prominently in binding the diphosphate Mycobacterium tuberculosis
evolution substrate recognition of bacterial and eukaryotic enzyme, involving a dynamic Arg, conserved steric interactions, and enzyme-substrate noncovalent interactions, overview. Domain 1 is important for positioning Galp for nucleophilic attack, domain 2 provides most of the interactions with the uridine group, and domain 3 figures prominently in binding the diphosphate Trypanosoma cruzi
evolution substrate recognition of bacterial and eukaryotic enzyme, involving a dynamic Arg, conserved steric interactions, and enzyme-substrate noncovalent interactions, overview. Domain 1 is important for positioning Galp for nucleophilic attack, domain 2 provides most of the interactions with the uridine group, and domain 3 figures prominently in binding the diphosphate Leishmania mexicana
evolution substrate recognition of bacterial and eukaryotic enzyme, involving a dynamic Arg, conserved steric interactions, and enzyme-substrate noncovalent interactions, overview. Domain 1 is important for positioning Galp for nucleophilic attack, domain 2 provides most of the interactions with the uridine group, and domain 3 figures prominently in binding the diphosphate Aspergillus fumigatus
evolution substrate recognition of bacterial and eukaryotic enzyme, involving a dynamic Arg, conserved steric interactions, and enzyme-substrate noncovalent interactions, overview. Domain 1 is important for positioning Galp for nucleophilic attack, domain 2 provides most of the interactions with the uridine group, and domain 3 figures prominently in binding the diphosphate Leishmania major
evolution substrate recognition of bacterial and eukaryotic enzyme, involving a dynamic Arg, conserved steric interactions, and enzyme-substrate noncovalent interactions, overview. Domain 1 is important for positioning Galp for nucleophilic attack, domain 2 provides most of the interactions with the uridine group, and domain 3 figures prominently in binding the diphosphate Leishmania infantum
evolution substrate recognition of bacterial and eukaryotic enzyme, involving a dynamic Arg, conserved steric interactions, and enzyme-substrate noncovalent interactions, overview. Domain 1 is important for positioning Galp for nucleophilic attack, domain 2 provides most of the interactions with the uridine group, and domain 3 figures prominently in binding the diphosphate Deinococcus radiodurans
evolution substrate recognition of bacterial and eukaryotic enzyme, involving a dynamic Arg, conserved steric interactions, and enzyme-substrate noncovalent interactions, overview. Domain 1 is important for positioning Galp for nucleophilic attack, domain 2 provides most of the interactions with the uridine group, and domain 3 figures prominently in binding the pyrophosphate Klebsiella pneumoniae
additional information molecular dynamics studies of active site flexibility, overview Escherichia coli
additional information molecular dynamics studies of active site flexibility, overview Klebsiella pneumoniae
additional information molecular dynamics studies of active site flexibility, overview Mycobacterium tuberculosis
additional information molecular dynamics studies of active site flexibility, overview Trypanosoma cruzi
additional information molecular dynamics studies of active site flexibility, overview Leishmania mexicana
additional information molecular dynamics studies of active site flexibility, overview Leishmania major
additional information molecular dynamics studies of active site flexibility, overview Leishmania infantum
additional information substrate recognition mechanism, overview. Molecular dynamics studies of active site flexibility, overview Aspergillus fumigatus
additional information substrate recognition mechanism, overview. Molecular dynamics studies of active site flexibility, overview Deinococcus radiodurans