EC Number |
BRENDA No. |
Title |
Journal |
Volume |
Pages |
Year |
Organism |
PubMed ID |
---|
4.1.1.85 | 672127 |
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 |
16489742 |
4.1.1.85 | 658080 |
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 |
15157078 |
4.1.1.85 | 658106 |
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 |
15697206 |
4.1.1.85 | 658106 |
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 |
Methylomonas aminofaciens |
15697206 |
4.1.1.85 | 658079 |
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 |
15157077 |
4.1.1.85 | 658107 |
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 |
15697207 |
4.1.1.85 | 650143 |
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 |
11900527 |
4.1.1.85 | 702041 |
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 |
19222992 |
4.1.1.85 | 702041 |
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 UA159 |
19222992 |
4.1.1.85 | 657958 |
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 |
14567674 |