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 (Cofactor
Cofactor on EC 5.4.99.9 - UDP-galactopyranose mutase
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COFACTOR 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
IMAGE
FADH2
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reduced FAD is required for activity. Reconstitution of apoenzyme with other FAD analogues, e.g. with methoxy-FAD, trifluoromethyl-FAD, or chloro-FAD, which are less effective than FAD, overview
FAD
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exists in a reduced state when the enzyme is catalytically active
FAD
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UGM is only catalytically active when the flavin is in the reduced form
FAD
a flavoenzyme, FAD is tightly bound, binding kinetics and mechanism
FAD
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enzyme UGM possesses a flavin adenine dinucleotide (FAD) cofactor that it uses to catalyze ring contraction of UDP-galactopyranose (UDP-Galp) to form UDP-galactofuranose (UDP-Galf)
FAD
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enzyme UGM possesses a flavin adenine dinucleotide (FAD) cofactor that it uses to catalyze ring contraction of UDP-galactopyranose (UDP-Galp) to form UDP-galactofuranose (UDP-Galf)
FAD
enzyme UGM possesses a flavin adenine dinucleotide (FAD) cofactor that it uses to catalyze ring contraction of UDP-galactopyranose (UDP-Galp) to form UDP-galactofuranose (UDP-Galf)
FAD
enzyme UGM possesses a flavin adenine dinucleotide (FAD) cofactor that it uses to catalyze ring contraction of UDP-galactopyranose (UDP-Galp) to form UDP-galactofuranose (UDP-Galf)
FAD
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involved in the catalyzed reaction, formation of a flavin-substrate/flavin-product adduct
FAD
structure analysis reveals UDP bound in the active site and galactopyranose linked to the FAD through a covalent bond between the anomeric C of galactopyranose and N5 of the FAD. The structure confirms the role of the flavin as nucleophile and supports the hypothesis that the proton destined for O5 of galactofuranose is shuttled from N5 of the FAD via O4 of the FAD
FAD
the flavin functions as a catalytic center in a non-redox reaction, catalytic function, overview. The flavin is required to be in the reduced state and functions as a nucleophile. The flavin must cycle back to the oxidized state for sustained catalysis
flavin
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flavoenzyme, conformational changes induced by flavin reduction, overview
flavin
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flavoenzyme, reduction of AfUGM also changes the conformation of the flavin itself, enzyme conformational changes induced by flavin reduction, overview
flavin
the flavin needs to be reduced for the enzyme to be active
additional information
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UGMs are active only in the reduced form
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additional information
UGMs are active only in the reduced form. Kinetic parameters for the reduction of AfUGM mutant enzymes by NADPH compared to wild-type enzyme, overview
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additional information
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UGMs are active only in the reduced form. Kinetic parameters for the reduction of AfUGM mutant enzymes by NADPH compared to wild-type enzyme, overview
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