EC Number |
BRENDA No. |
Title |
Journal |
Volume |
Pages |
Year |
Organism |
PubMed ID |
---|
3.1.3.45 | 749511 |
A preliminary X-ray study of 3-deoxy-D-manno-oct-2-ulosonic acid 8-phosphate phosphatase (YrbI) from Burkholderia pseudomallei |
Acta Crystallogr. Sect. F |
71 |
790-793 |
2015 |
Burkholderia pseudomallei |
- |
3.1.3.45 | 749491 |
Ligand-bound structures of 3-deoxy-D-manno-octulosonate 8-phosphate phosphatase from Moraxella catarrhalis reveal a water channel connecting to the active site for the second step of catalysis |
Acta Crystallogr. Sect. D |
71 |
239-255 |
2015 |
Moraxella catarrhalis |
25664734 |
3.1.3.45 | 749491 |
Ligand-bound structures of 3-deoxy-D-manno-octulosonate 8-phosphate phosphatase from Moraxella catarrhalis reveal a water channel connecting to the active site for the second step of catalysis |
Acta Crystallogr. Sect. D |
71 |
239-255 |
2015 |
Moraxella catarrhalis BC8 |
25664734 |
3.1.3.45 | 646345 |
Anomeric specificity of 3-deoxy-D-manno-2-octulosonate 8-phosphate phosphatase from Escherichia coli |
J. Am. Chem. Soc. |
112 |
4972-4974 |
1990 |
Escherichia coli |
- |
3.1.3.45 | 652389 |
Escherichia coli YrbI is 3-deoxy-D-manno-octulosonate 8-phosphate phosphatase |
J. Biol. Chem. |
278 |
18117-18123 |
2003 |
Escherichia coli |
12639950 |
3.1.3.45 | 682819 |
Non-essential KDO biosynthesis and new essential cell envelope biogenesis genes in the Escherichia coli yrbG-yhbG locus |
Res. Microbiol. |
157 |
547-558 |
2006 |
Escherichia coli |
16765569 |
3.1.3.45 | 646344 |
Purification and characterization of a specific 3-deoxy-D-manno-octulosonate 8-phosphate phosphatase from Escherichia coli B |
J. Bacteriol. |
142 |
60-68 |
1980 |
Escherichia coli |
6246070 |
3.1.3.45 | 646344 |
Purification and characterization of a specific 3-deoxy-D-manno-octulosonate 8-phosphate phosphatase from Escherichia coli B |
J. Bacteriol. |
142 |
60-68 |
1980 |
Escherichia coli B / ATCC 11303 |
6246070 |
3.1.3.45 | 729235 |
Structural basis for the divergence of substrate specificity and biological function within HAD phosphatases in lipopolysaccharide and sialic acid biosynthesis |
Biochemistry |
52 |
5372-5386 |
2013 |
Bacteroides thetaiotaomicron |
23848398 |
3.1.3.45 | 729235 |
Structural basis for the divergence of substrate specificity and biological function within HAD phosphatases in lipopolysaccharide and sialic acid biosynthesis |
Biochemistry |
52 |
5372-5386 |
2013 |
Haemophilus influenzae |
23848398 |