Reference on EC 4.1.1.85 - 3-dehydro-L-gulonate-6-phosphate decarboxylase
Please use the Reference Search for a specific query.
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
REF. 
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Wise, E.; Yew, W.S.; Babbitt, P.C.; Gerlt, J.A.; Rayment, I.
Homologous (beta/alpha)8-barrel enzymes that catalyze unrelated reactions: orotidine 5'-monophosphate decarboxylase and 3-keto-L-gulonate 6-phosphate decarboxylase
Biochemistry
41
3861-3869
2002
Escherichia coli (P39304), Escherichia coli
Wise, E.L.; Yew, W.S.; Gerlt, J.A.; Rayment, I.
Structural evidence for a 1,2-enediolate intermediate in the reaction catalyzed by 3-keto-L-gulonate 6-phosphate decarboxylase, a member of the orotidine 5'-monophosphate decarboxylase suprafamily
Biochemistry
42
12133-12142
2003
Escherichia coli (P39304)
Yew, W.S.; Wise, E.L.; Rayment, I.; Gerlt, J.A.
Evolution of enzymatic activities in the orotidine 5'-monophosphate decarboxylase suprafamily: mechanistic evidence for a proton relay system in the active site of 3-keto-L-gulonate 6-phosphate decarboxylase
Biochemistry
43
6427-6437
2004
Escherichia coli K-12
Wise, E.L.; Yew, W.S.; Gerlt, J.A.; Rayment, I.
Evolution of enzymatic activities in the orotidine 5'-monophosphate decarboxylase suprafamily: crystallographic evidence for a proton relay system in the active site of 3-keto-L-gulonate 6-phosphate decarboxylase
Biochemistry
43
6438-6446
2004
Escherichia coli (P39304)
Yew, W.S.; Akana, J.; Wise, E.L.; Rayment, I.; Gerlt, J.A.
Evolution of enzymatic activities in the orotidine 5'-monophosphate decarboxylase suprafamily: enhancing the promiscuous D-arabino-hex-3-ulose 6-phosphate synthase reaction catalyzed by 3-keto-L-gulonate 6-phosphate decarboxylase
Biochemistry
44
1807-1815
2005
Escherichia coli K-12, Methylomonas aminofaciens
Wise, E.L.; Yew, W.S.; Akana, J.; Gerlt, J.A.; Rayment, I.
Evolution of enzymatic activities in the orotidine 5'-monophosphate decarboxylase suprafamily: structural basis for catalytic promiscuity in wild-type and designed mutants of 3-keto-L-gulonate 6-phosphate decarboxylase
Biochemistry
44
1816-1823
2005
Escherichia coli K-12 (P39304)
Yew, W.S.; Gerlt, J.A.
Utilization of L-ascorbate by Escherichia coli K-12: assignments of functions to products of the yjf-sga and yia-sgb operons
J. Bacteriol.
184
302-306
2002
Escherichia coli K-12
Akana, J.; Fedorov, A.A.; Fedorov, E.; Novak, W.R.; Babbitt, P.C.; Almo, S.C.; Gerlt, J.A.
D-Ribulose 5-phosphate 3-epimerase: functional and structural relationships to members of the ribulose-phosphate binding (beta/alpha)8-barrel superfamily
Biochemistry
45
2493-2503
2006
Escherichia coli
Li, G.L.; Liu, X.; Nan, J.; Brostromer, E.; Li, L.F.; Su, X.D.
Open-closed conformational change revealed by the crystal structures of 3-keto-L-gulonate 6-phosphate decarboxylase from Streptococcus mutans
Biochem. Biophys. Res. Commun.
381
429-433
2009
Streptococcus mutans, Streptococcus mutans UA159
html completed
