Results 131 to 140 of about 819,741 (161)

Human TBC1 domain-containing kinase is a class I multidomain pseudokinase. [PDF]

open access: yesProtein Expr Purif
Maurya S, Cheek LE, Iavarone AT, Zhu W.
europepmc   +1 more source

Pentaphosphorylated magic spot nucleotides: chemoenzymatic synthesis and disassembly-based sensing.

open access: yesOrg Biomol Chem
Moser P   +6 more
europepmc   +1 more source

Isoleucine 259 and Isoleucine 260 Residues in Streptococcus gordonii Soluble Inorganic Pyrophosphatase Play an Important Role in Enzyme Activity

open access: yesJournal of Bioscience and Bioengineering, 2011
The hinge region of the family II soluble inorganic pyrophosphatase (PPase) found in Streptococcus gordonii DL1 (Challis) has previously been shown to play an important role in opening and closing of the active site between the N- and C-terminal domains of PPase.
Scott A White, Mohammad Ilias
exaly   +4 more sources

Streptococcus gordonii Soluble Inorganic Pyrophosphatase: An Important Role for the Interdomain Region in Enzyme Activity

Biochimica Et Biophysica Acta - Proteins and Proteomics, 2006
Streptococcus gordonii DL1(Challis) soluble inorganic pyrophosphatase was shown to be a homo dimer with a subunit molecular mass of 33407. In solution, in the presence of Mn(2+), the protein is ellipsoidal with an axial ratio of 3.37 and molecular mass of 67000.
Mohammad Ilias
exaly   +3 more sources

Evidence for a Non-Overlapping Subcellular Localization of the Family I Isoforms of Soluble Inorganic Pyrophosphatase in Arabidopsis thaliana

Plant Science, 2016
Pyrophosphate is a byproduct of macromolecular biosynthesis and its degradation gives a thermodynamic impulse to cell growth. Soluble inorganic pyrophosphatases (PPa) are present in all living cells, but in plants and other Eukaryotes membrane-bound H+-pumping pyrophosphatases may compete with these soluble counterparts for the substrate.
Sonia Vazquez-Santana   +2 more
exaly   +3 more sources

Characterization of a Soluble Inorganic Pyrophosphatase From Microcystis aeruginosa and Preparation of Its Antibody

Archives of Biochemistry and Biophysics, 1991
A soluble inorganic pyrophosphatase was isolated from a crude extract of Microcystis aeruginosa by adsorption chromatography. The enzyme was purified to homogeneity as judged by sodium dodecyl sulfate (SDS) and nondenaturing polyacrylamide gel electrophoresis and N-terminal amino acid analysis.
Kang, C.B.H., Ho, K.K.
exaly   +3 more sources

Expression and Evolutionary Analysis of Soluble Inorganic Pyrophosphatase Gene Family in Pear and Four Other Rosaceae Species

Plant Systematics and Evolution, 2020
In plants, soluble inorganic pyrophosphatase (PPA) play an indispensable role in inorganic pyrophosphate hydrolysis. However, the expression and the evolutionary history of PPA gene family remain unclear in pear and Rosaceae species. In this study, thirty-nine PPA genes were identified from five Rosaceae species including pear (Pyrus bretschneideri ...
Juyou Wu, Shaoling Zhang, Xin Qiao
exaly   +2 more sources

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