5.4.99.9: UDP-galactopyranose mutase
This is an abbreviated version!
For detailed information about UDP-galactopyranose mutase, go to the full flat file.
Word Map on EC 5.4.99.9
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5.4.99.9
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phosphoglycerate
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methylmalonic
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methylmalonyl-coa
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udp-galactofuranose
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galactofuranose
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chorismate
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urogenital
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udp-galf
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acidemia
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galf
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adenosylcobalamin
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methylmalonyl-coenzyme
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sinus
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prephenate
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acidurias
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succinyl-coa
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b12-dependent
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2,3-bisphosphoglycerate
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bisphosphoglycerate
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flavoenzyme
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adocbl
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cobalamin-dependent
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propionyl-coa
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adenosylcobalamin-dependent
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drug development
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isobutyryl-coa
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cofactor-dependent
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shermanii
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cytodifferentiation
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methylcobalamin
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phosphoenzyme
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cobiialamin
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analysis
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medicine
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synthesis
- 5.4.99.9
- phosphoglycerate
-
methylmalonic
- methylmalonyl-coa
- udp-galactofuranose
-
galactofuranose
- chorismate
-
urogenital
-
udp-galf
- acidemia
-
galf
- adenosylcobalamin
-
methylmalonyl-coenzyme
-
sinus
- prephenate
- acidurias
- succinyl-coa
-
b12-dependent
- 2,3-bisphosphoglycerate
-
bisphosphoglycerate
-
flavoenzyme
-
adocbl
-
cobalamin-dependent
- propionyl-coa
-
adenosylcobalamin-dependent
- drug development
- isobutyryl-coa
-
cofactor-dependent
- shermanii
-
cytodifferentiation
- methylcobalamin
- phosphoenzyme
-
cobiialamin
- analysis
- medicine
- synthesis
Reaction
Synonyms
AfUGM, ANIA_03112, CdUGM, galactopyranose mutase, Glf, GLF gene product, GLF-1, glfA, MtUGM, mutase, Mutase, uridine diphosphogalactopyranose, TcUGM, UDP galactopyranose mutase, UDP-D-galactopyranose mutase, UDP-Gal mutase, UDP-galactopyranose mutase, UDP-Galp mutase, UGM, UgmA, UNGM, uridine 5'-diphosphate galactopyranose mutase, uridine 5'-diphosphate galactopyranosemutase, uridine 5'-diphosphate-galactopyranose mutase, uridine diphosphate galactopyranose mutase
ECTree
5.4.99.9 UDP-galactopyranose mutaseAdvanced search results
results (
results (Engineering
Engineering on EC 5.4.99.9 - UDP-galactopyranose mutase
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PROTEIN VARIANTS 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
F66A
H63N
N207A
site-directed mutagenesis, the mutant enzyme shows a high decrease in kcat/KM value compared to wild-type, but the mutation does not significantly affect the kinetics of enzyme activation by NADPH. Crystal structure determination of the enzyme ligand-free or in complex with UDP
Q107A
site-directed mutagenesis, the mutant enzyme shows a high decrease in kcat/KM value compared to wild-type, but the mutation does not significantly affect the kinetics of enzyme activation by NADPH. Crystal structure determination of the ligand-free enzyme
R182A
R182K
R327A
R327K
W315A
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme. The extra space afforded by the absence of the Trp315 wall possibly lowers the free energy barrier of the cyclization step of the catalytic mechanism, allowing product release to become rate-limiting
Y104A
site-directed mutagenesis, the mutant enzyme shows a high decrease in kcat/KM value compared to wild-type, but the mutation does not significantly affect the kinetics of enzyme activation by NADPH. Crystal structure determination of the ligand-free enzyme
Y317A
site-directed mutagenesis, the mutant enzyme shows a high decrease in kcat/KM value compared to wild-type, but the mutation does not significantly affect the kinetics of enzyme activation by NADPH. Crystal structure determination of the enzyme ligand-free or in complex with UDP
D351A
mutation of conserved residue of putative active site cleft. 4% of wild-type activity
E301A
mutation of conserved residue of putative active site cleft. 21% of wild-type activity
R280A
mutation of conserved residue of putative active site cleft. No catalytic activity
W160A
W70F/W290F
D322A
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site-directed mutagenesis, the mutant shows altered kinetics compared to the wild-type with substrate UDP-alpha-D-galactofuranose
H68A
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site-directed mutagenesis, the mutant shows highly reduced catalytic efficiency compared to wild-type
P306R
site-directed mutagenesis, the mutant shows similar kinetics compared to wild-type. Pro306 is located on the solvent-exposed loop (His300-Lys309) connecting the small helix nu3 and beta strand beta14 of the beta-sheet domain, over 25 A from the FAD. The Cdelta atom of Pro306 is 3.5 A from the main-chain oxygen of Thr53, located on the small sharp turn (Glu52-Gly56) connecting beta strands beta3 and beta4.The Pro306Arg mutation releases this clash and results in a 1 A shift in the position of the two solvent-exposed loops without affecting the position of side chains and interaction with the protein. Arg306 forms a salt bridge with the side chain of Asp308 and the main-chain oxygen of Gln54 and replaces a salt bridge formed by Lys309. The Lys309 side chain has rotated and forms a new salt bridge with Gln54. In addition, Lys309 is involved in crystal contacts with the side chain of Asp202. The Pro306Ala mutation therefore may be stabilizing the two loops and promoting the crystallization of MtUGM complex structures
Y253A
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site-directed mutagenesis, the mutant shows altered kinetics compared to the wild-type with substrate UDP-alpha-D-galactofuranose
N201A
site-directed mutagenesis, the mutant shows highly reduced catalytic efficiency compared to wild-type
Q103A
site-directed mutagenesis, the mutant shows highly reduced catalytic efficiency compared to wild-type
R176A
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site-directed mutagenesis, the mutant shows highly reduced activity compared to the wild-type enzyme
R327A
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site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
Y100A
site-directed mutagenesis, the mutant shows highly reduced catalytic efficiency compared to wild-type
Y317F
Y395F
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site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
Y429F
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site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
additional information
F66A
site-directed mutagenesis, the mutant enzyme shows a high decrease in kcat/KM value compared to wild-type, but the mutation does not significantly affect the kinetics of enzyme activation by NADPH. Crystal structure determination of the enzyme ligand-free or in complex with UDP or UDP and substrate UDP-alpha-D-galactopyranose
F66A
site-directed mutagenesis, the residue is located at the end of AfUgmA loop III and may control loop III flipping and consequently opening of the mobile loops depending on the redox state of the cofactor. The colony morphology, cell wall composition, hyphal surface adhesion and response to antifungal drugs of the mutant are altered compared to wild-type
H63N
site-directed mutagenesis, the residue is part of the flexible loop (loop III) above the si-face of the isoalloxazine ring. The colony morphology, cell wall composition, hyphal surface adhesion and response to antifungal drugs of the mutant are altered compared to wild-type
H63N
site-directed mutagenesis, the structure of enzyme mutant AfUGMH63A complexed with the substrate UDP-Galp shows the presence of a C1-galactose-N5-FAD adduct (PDB ID 5HHF)
R182A
site-directed mutagenesis, the colony morphology, cell wall composition, hyphal surface adhesion and response to antifungal drugs of the mutant are altered compared to wild-type
R182K
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
R182K
site-directed mutagenesis, the colony morphology, cell wall composition, hyphal surface adhesion and response to antifungal drugs of the mutant are altered compared to wild-type
R327A
site-directed mutagenesis, the colony morphology, cell wall composition, hyphal surface adhesion and response to antifungal drugs of the mutant are altered compared to wild-type
R327K
site-directed mutagenesis, the mutant shows highly reduced activity compared to the wild-type enzyme
R327K
site-directed mutagenesis, the colony morphology, cell wall composition, hyphal surface adhesion and response to antifungal drugs of the mutant are altered compared to wild-type
W160A
mutation of conserved residue on edge putative active site cleft, defective in binding of substrate
W160A
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redox-switched binding affinity of substrate reverses in the W160A mutant where it only binds when oxidized
W70F/W290F
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wild type UGM and the W70F/W290F double mutant show competition of UDP and UDP-galactopyranose for the same site
W70F/W290F
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the double mutant binds substrate in a similar manner to wild type and has comparable enzyme activity (90%)
Y317F
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site-directed mutagenesis, the mutant shows highly reduced activity compared to the wild-type enzyme
Y317F
site-directed mutagenesis, the mutant shows highly reduced catalytic efficiency compared to wild-type
additional information
kinetic parameters for the reduction of AfUGM mutant enzymes by NADPH compared to wild-type enzyme, overview
additional information
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kinetic parameters for the reduction of AfUGM mutant enzymes by NADPH compared to wild-type enzyme, overview
additional information
the AfUgmA enzyme deletion mutant shows increased sensitivity to antifungal drugs, particularly caspofungin. Reduced beta-glucan content is correlated with increased caspofungin sensitivity
additional information
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the AfUgmA enzyme deletion mutant shows increased sensitivity to antifungal drugs, particularly caspofungin. Reduced beta-glucan content is correlated with increased caspofungin sensitivity
additional information
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compared to a wild type morphology strain, the UGM-deficient ugmA? strain has aberrant hyphal morphology, producing wide, uneven, highly-branched hyphae, with thick, relatively electron-dense walls
additional information
Construction of an AnugmADELTA enzyme deletion mutant. An Aspergillus fumigatus enzyme AfUgmA mutant with altered enzyme activity is transformed into enzyme-lacking Aspergillus nidulans mutant AnugmDELTA to assess the effect on growth and wall composition in Aspergillus nidulans. The complemented AnugmA::wild-type AfugmA strain has wild-type phenotype. Aspergillus nidulans strains that host mutated AfUgmA constructs with low enzyme activity show increased hyphal surface adhesion, and AnugmAn and AfugmA-mutated Aspergillus nidulans strains have increased alpha-glucan and decreased beta-glucan in their cell walls compared to wild-type and AfugmA-complemented strains
additional information
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Construction of an AnugmADELTA enzyme deletion mutant. An Aspergillus fumigatus enzyme AfUgmA mutant with altered enzyme activity is transformed into enzyme-lacking Aspergillus nidulans mutant AnugmDELTA to assess the effect on growth and wall composition in Aspergillus nidulans. The complemented AnugmA::wild-type AfugmA strain has wild-type phenotype. Aspergillus nidulans strains that host mutated AfUgmA constructs with low enzyme activity show increased hyphal surface adhesion, and AnugmAn and AfugmA-mutated Aspergillus nidulans strains have increased alpha-glucan and decreased beta-glucan in their cell walls compared to wild-type and AfugmA-complemented strains
additional information
Aspergillus nidulans FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139
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Construction of an AnugmADELTA enzyme deletion mutant. An Aspergillus fumigatus enzyme AfUgmA mutant with altered enzyme activity is transformed into enzyme-lacking Aspergillus nidulans mutant AnugmDELTA to assess the effect on growth and wall composition in Aspergillus nidulans. The complemented AnugmA::wild-type AfugmA strain has wild-type phenotype. Aspergillus nidulans strains that host mutated AfUgmA constructs with low enzyme activity show increased hyphal surface adhesion, and AnugmAn and AfugmA-mutated Aspergillus nidulans strains have increased alpha-glucan and decreased beta-glucan in their cell walls compared to wild-type and AfugmA-complemented strains
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additional information
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gene replacement mutant is deficient in lipophosphoglycan backbone and expresses truncated glycoinositolphospholipids. The structural changes do not influence the in vitro growth but lead to an attenuation of virulence
