EC Number   |
General Information |
Reference |
|---|
    3.6.1.1 | evolution |
AtPPsPase1 belongs to the haloacid dehalogenase, HAD, superfamily |
-, 718979 |
| 3.6.1.1 | evolution |
enzyme BT2127 is a member of the haloalkanoate dehalogenase superfamily, HADSF |
-, 718917 |
| 3.6.1.1 | evolution |
family II soluble inorganic pyrophosphatase |
-, 720075 |
| 3.6.1.1 | evolution |
hierarchical clustering and three-dimensional (3D) homology modeling reveals that HvPPA is distinct in structure from characterized inorganic diphosphatases, PPAs. HvPPA beongs to the class A type inorganic diphosphatases, PPAs. Evolutionary relationships of archaeal PPAs, overview |
755844 |
| 3.6.1.1 | evolution |
Mycobacterium tuberculosis and Mycobacterium leprae genomes include genes for the only two family I inorganic pyrophosphatases known to contain two histidines in the active site, structure comparison of family I enzymes, overview |
-, 718514 |
| 3.6.1.1 | evolution |
PPases include membrane associated V-H+-PPases (vacuolar H+-translocating PPases) and soluble form PPases, where latter comprise two families that differ in their sequence and structure. Family I PPases are Mg2+ dependent enzymes known to exist as homo-hexamers in prokaryotes and dimers in eukaryotes6. Family II PPases are Mn2+-dependent enzymes with bi-domain structures, and active in dimeric or trimeric forms. Structure comparisons of the enzyme from Plasmodium falciparum (PfPPase) and Toxoplasma gondii (TgPPase), overview. Comparison of eukaryotic family I PPases reveal diversity in dimerization modes |
758414 |
| 3.6.1.1 | evolution |
PPases include membrane associated V-H+-PPases (vacuolar H+-translocating PPases) and soluble form PPases, where latter comprise two families that differ in their sequence and structure6. Family I PPases are Mg2+ dependent enzymes known to exist as homo-hexamers in prokaryotes and dimers in eukaryotes. Family II PPases are Mn2+ dependent enzymes with bi-domain structures, and active in dimeric or trimeric forms. Structure comparisons of the enzyme from Plasmodium falciparum (PfPPase) and Toxoplasma gondii (TgPPase), overview. Comparison of eukaryotic family I PPases reveals diversity in dimerization modes |
758414 |
| 3.6.1.1 | evolution |
soluble PPases belong to three nonhomologous families, of which family II is found in approximately a quarter of prokaryotic organisms, often pathogenic ones. Each subunit of dimeric canonical Family II PPases is formed by two domains connected by a flexible linker, with the active site located between the domains. The enzymes require both magnesium and a transition metal ion (manganese or cobalt) for maximal activity and are the most active among all PPase types. Soluble PPases convert diphosphate energy into heat, as opposed to membrane-bound PPases, which employ diphosphate energy to transport H+ or Na+ across membranes in plants and some bacteria, archaea, and protists. Soluble PPases belong to three nonhomologous families, I, II, and III. Family I PPases are found in all kingdoms of life, whereas Family II and Family III PPases are found in prokaryotes. Distribution of Family II PPases, overview |
-, 756721 |
| 3.6.1.1 | evolution |
soluble PPases belong to three nonhomologous families, of which family II is found in approximately a quarter of prokaryotic organisms, often pathogenic ones. The enzymes require both magnesium and a transition metal ion (manganese or cobalt) for maximal activity and are the most active among all PPase types. Soluble PPases convert diphosphate energy into heat, as opposed to membrane-bound PPases, which employ diphosphate energy to transport H+ or Na+ across membranes in plants and some bacteria, archaea, and protists. Soluble PPases belong to three nonhomologous families, I, II, and III. Family I PPases are found in all kingdoms of life, whereas Family II and Family III PPases are found in prokaryotes. Distribution of Family II PPases, overview |
756721 |
| 3.6.1.1 | evolution |
the enzyme belongs to the CBS-PPases |
-, 755998 |
