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Literature summary extracted from
- Structure, mechanism, and dynamics of UDP-galactopyranose mutase (2014), Arch. Biochem. Biophys., 544, 128-141.
Activating Compound
| EC Number | Activating Compound | Comment | Organism | Structure |
|---|---|---|---|---|
| 5.4.99.9 | additional information | enzyme activation mechanism, overview | Trypanosoma cruzi | |
| 5.4.99.9 | additional information | enzyme activation mechanism, overview | Aspergillus fumigatus | |
| 5.4.99.9 | additional information | enzme activation mechanism, overview | Klebsiella pneumoniae | |
| 5.4.99.9 | additional information | enzme activation mechanism, overview | Deinococcus radiodurans | |
| 5.4.99.9 | NAD(P)H | enzyme activation mechanism, overview | Escherichia coli |  |
| 5.4.99.9 | 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 | |
| 5.4.99.9 | 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 | |
| 5.4.99.9 | 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 | |
| 5.4.99.9 | 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 | |
| 5.4.99.9 | 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)
| EC Number | Crystallization (Comment) | Organism |
|---|---|---|
| 5.4.99.9 | crystal structure analysis | Escherichia coli |
| 5.4.99.9 | crystal structure analysis | Klebsiella pneumoniae |
| 5.4.99.9 | crystal structure analysis | Mycobacterium tuberculosis |
| 5.4.99.9 | crystal structure analysis | Trypanosoma cruzi |
| 5.4.99.9 | crystal structure analysis | Deinococcus radiodurans |
| 5.4.99.9 | crystal structure analysis, two crystal forms, hexagonal and triclinic | Aspergillus fumigatus |
Natural Substrates/ Products (Substrates)
| EC Number | Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 5.4.99.9 | UDP-alpha-D-galactopyranose | Escherichia coli | - |
UDP-alpha-D-galactofuranose | - |
r | |
| 5.4.99.9 | UDP-alpha-D-galactopyranose | Klebsiella pneumoniae | - |
UDP-alpha-D-galactofuranose | - |
r | |
| 5.4.99.9 | UDP-alpha-D-galactopyranose | Mycobacterium tuberculosis | - |
UDP-alpha-D-galactofuranose | - |
r | |
| 5.4.99.9 | UDP-alpha-D-galactopyranose | Trypanosoma cruzi | - |
UDP-alpha-D-galactofuranose | - |
r | |
| 5.4.99.9 | UDP-alpha-D-galactopyranose | Leishmania mexicana | - |
UDP-alpha-D-galactofuranose | - |
r | |
| 5.4.99.9 | UDP-alpha-D-galactopyranose | Aspergillus fumigatus | - |
UDP-alpha-D-galactofuranose | - |
r | |
| 5.4.99.9 | UDP-alpha-D-galactopyranose | Leishmania major | - |
UDP-alpha-D-galactofuranose | - |
r | |
| 5.4.99.9 | UDP-alpha-D-galactopyranose | Leishmania infantum | - |
UDP-alpha-D-galactofuranose | - |
r | |
| 5.4.99.9 | UDP-alpha-D-galactopyranose | Deinococcus radiodurans | - |
UDP-alpha-D-galactofuranose | - |
r | |
| 5.4.99.9 | UDP-alpha-D-galactopyranose | Deinococcus radiodurans R1 / ATCC 13939 / DSM 20539 | - |
UDP-alpha-D-galactofuranose | - |
r | |
Organism
| EC Number | Organism | UniProt | Comment | Textmining |
|---|---|---|---|---|
| 5.4.99.9 | Aspergillus fumigatus | - |
- |
- |
| 5.4.99.9 | Deinococcus radiodurans | - |
- |
- |
| 5.4.99.9 | Deinococcus radiodurans R1 / ATCC 13939 / DSM 20539 | - |
- |
- |
| 5.4.99.9 | Escherichia coli | - |
- |
- |
| 5.4.99.9 | Klebsiella pneumoniae | - |
- |
- |
| 5.4.99.9 | Leishmania infantum | - |
- |
- |
| 5.4.99.9 | Leishmania major | - |
- |
- |
| 5.4.99.9 | Leishmania mexicana | - |
- |
- |
| 5.4.99.9 | Mycobacterium tuberculosis | - |
- |
- |
| 5.4.99.9 | Trypanosoma cruzi | - |
- |
- |
Reaction
| EC Number | Reaction | Comment | Organism | Reaction ID |
|---|---|---|---|---|
| 5.4.99.9 | UDP-alpha-D-galactopyranose = UDP-alpha-D-galactofuranose | chemical reaction mechanism, overview | Escherichia coli | |
| 5.4.99.9 | UDP-alpha-D-galactopyranose = UDP-alpha-D-galactofuranose | chemical reaction mechanism, overview | Klebsiella pneumoniae | |
| 5.4.99.9 | UDP-alpha-D-galactopyranose = UDP-alpha-D-galactofuranose | chemical reaction mechanism, overview | Trypanosoma cruzi | |
| 5.4.99.9 | UDP-alpha-D-galactopyranose = UDP-alpha-D-galactofuranose | chemical reaction mechanism, overview | Aspergillus fumigatus | |
| 5.4.99.9 | UDP-alpha-D-galactopyranose = UDP-alpha-D-galactofuranose | chemical reaction mechanism, overview | Deinococcus radiodurans |
Substrates and Products (Substrate)
| EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 5.4.99.9 | UDP-alpha-D-galactopyranose | - |
Escherichia coli | UDP-alpha-D-galactofuranose | - |
r | |
| 5.4.99.9 | UDP-alpha-D-galactopyranose | - |
Klebsiella pneumoniae | UDP-alpha-D-galactofuranose | - |
r | |
| 5.4.99.9 | UDP-alpha-D-galactopyranose | - |
Mycobacterium tuberculosis | UDP-alpha-D-galactofuranose | - |
r | |
| 5.4.99.9 | UDP-alpha-D-galactopyranose | - |
Trypanosoma cruzi | UDP-alpha-D-galactofuranose | - |
r | |
| 5.4.99.9 | UDP-alpha-D-galactopyranose | - |
Leishmania mexicana | UDP-alpha-D-galactofuranose | - |
r | |
| 5.4.99.9 | UDP-alpha-D-galactopyranose | - |
Aspergillus fumigatus | UDP-alpha-D-galactofuranose | - |
r | |
| 5.4.99.9 | UDP-alpha-D-galactopyranose | - |
Leishmania major | UDP-alpha-D-galactofuranose | - |
r | |
| 5.4.99.9 | UDP-alpha-D-galactopyranose | - |
Leishmania infantum | UDP-alpha-D-galactofuranose | - |
r | |
| 5.4.99.9 | UDP-alpha-D-galactopyranose | - |
Deinococcus radiodurans | UDP-alpha-D-galactofuranose | - |
r | |
| 5.4.99.9 | 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 | |
| 5.4.99.9 | 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 | |
| 5.4.99.9 | 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 | |
| 5.4.99.9 | 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 | |
| 5.4.99.9 | 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 | |
| 5.4.99.9 | 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 | |
| 5.4.99.9 | 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 | |
| 5.4.99.9 | 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 | |
| 5.4.99.9 | 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 | |
| 5.4.99.9 | UDP-alpha-D-galactopyranose | - |
Deinococcus radiodurans R1 / ATCC 13939 / DSM 20539 | UDP-alpha-D-galactofuranose | - |
r | |
| 5.4.99.9 | 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
| EC Number | Subunits | Comment | Organism |
|---|---|---|---|
| 5.4.99.9 | decamer | pentamer-of-dimers, in crystals | Deinococcus radiodurans |
| 5.4.99.9 | dimer | in solution | Deinococcus radiodurans |
| 5.4.99.9 | 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 |
| 5.4.99.9 | 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 |
| 5.4.99.9 | 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 |
| 5.4.99.9 | monomer | the unique fold-level variations exhibited by TcUGM are responsible for the monomeric state | Trypanosoma cruzi |
| 5.4.99.9 | More | oligomeric state and quaternary structure, overview | Trypanosoma cruzi |
| 5.4.99.9 | More | the tertiary structure dictates the oligomeric state, oligomeric state and quaternary structure, overview | Aspergillus fumigatus |
| 5.4.99.9 | 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
| EC Number | Synonyms | Comment | Organism |
|---|---|---|---|
| 5.4.99.9 | UGM | - |
Escherichia coli |
| 5.4.99.9 | UGM | - |
Klebsiella pneumoniae |
| 5.4.99.9 | UGM | - |
Mycobacterium tuberculosis |
| 5.4.99.9 | UGM | - |
Trypanosoma cruzi |
| 5.4.99.9 | UGM | - |
Leishmania mexicana |
| 5.4.99.9 | UGM | - |
Aspergillus fumigatus |
| 5.4.99.9 | UGM | - |
Leishmania major |
| 5.4.99.9 | UGM | - |
Leishmania infantum |
| 5.4.99.9 | UGM | - |
Deinococcus radiodurans |
pH Optimum
| EC Number | pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|---|
| 5.4.99.9 | 7 | - |
assay at | Escherichia coli |
| 5.4.99.9 | 7 | - |
assay at | Klebsiella pneumoniae |
| 5.4.99.9 | 7 | - |
assay at | Mycobacterium tuberculosis |
| 5.4.99.9 | 7 | - |
assay at | Trypanosoma cruzi |
| 5.4.99.9 | 7 | - |
assay at | Leishmania mexicana |
| 5.4.99.9 | 7 | - |
assay at | Aspergillus fumigatus |
| 5.4.99.9 | 7 | - |
assay at | Leishmania major |
| 5.4.99.9 | 7 | - |
assay at | Leishmania infantum |
| 5.4.99.9 | 7 | - |
assay at | Deinococcus radiodurans |
Cofactor
| EC Number | Cofactor | Comment | Organism | Structure |
|---|---|---|---|---|
| 5.4.99.9 | flavin | flavoenzyme | Klebsiella pneumoniae | |
| 5.4.99.9 | flavin | flavoenzyme | Mycobacterium tuberculosis | |
| 5.4.99.9 | flavin | flavoenzyme | Leishmania mexicana | |
| 5.4.99.9 | flavin | flavoenzyme | Leishmania major | |
| 5.4.99.9 | flavin | flavoenzyme | Leishmania infantum | |
| 5.4.99.9 | flavin | flavoenzyme | Deinococcus radiodurans | |
| 5.4.99.9 | flavin | flavoenzyme, conformational changes induced by flavin reduction, overview | Trypanosoma cruzi | |
| 5.4.99.9 | flavin | flavoenzyme, reduction of AfUGM also changes the conformation of the flavin itself, enzyme conformational changes induced by flavin reduction, overview | Aspergillus fumigatus | |
| 5.4.99.9 | flavin | flavoenzyme, required for enzyme activation mechanism, overview | Escherichia coli | |
General Information
| EC Number | General Information | Comment | Organism |
|---|---|---|---|
| 5.4.99.9 | 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 |
| 5.4.99.9 | 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 |
| 5.4.99.9 | 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 |
| 5.4.99.9 | 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 |
| 5.4.99.9 | 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 |
| 5.4.99.9 | 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 |
| 5.4.99.9 | 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 |
| 5.4.99.9 | 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 |
| 5.4.99.9 | 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 |
| 5.4.99.9 | additional information | molecular dynamics studies of active site flexibility, overview | Escherichia coli |
| 5.4.99.9 | additional information | molecular dynamics studies of active site flexibility, overview | Klebsiella pneumoniae |
| 5.4.99.9 | additional information | molecular dynamics studies of active site flexibility, overview | Mycobacterium tuberculosis |
| 5.4.99.9 | additional information | molecular dynamics studies of active site flexibility, overview | Trypanosoma cruzi |
| 5.4.99.9 | additional information | molecular dynamics studies of active site flexibility, overview | Leishmania mexicana |
| 5.4.99.9 | additional information | molecular dynamics studies of active site flexibility, overview | Leishmania major |
| 5.4.99.9 | additional information | molecular dynamics studies of active site flexibility, overview | Leishmania infantum |
| 5.4.99.9 | additional information | substrate recognition mechanism, overview. Molecular dynamics studies of active site flexibility, overview | Aspergillus fumigatus |
| 5.4.99.9 | additional information | substrate recognition mechanism, overview. Molecular dynamics studies of active site flexibility, overview | Deinococcus radiodurans |
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