Disease relevance of IPP1

• In Escherichia coli PPase, the enzyme.PP(i) intermediate binds F(-) rapidly, explaining the lack of time dependence in the inhibition of this enzyme [1].
• Purification and properties of inorganic pyrophosphatase of rat liver and hepatoma 3924A [2].
• Comparative kinetic studies on the two interconvertible forms of Streptococcus faecalis inorganic pyrophosphatase [3].
• Characterization of a soluble inorganic pyrophosphatase from Microcystis aeruginosa and preparation of its antibody [4].
• The purified virions also contain an inorganic pyrophosphatase activity [5].

High impact information on IPP1

• Evolutionary conservation of the active site of soluble inorganic pyrophosphatase [6].
• A second region of the pnk sequence shares homology with phosphoglycerate kinase, yeast inorganic pyrophosphatase and histone 2b from various organisms [7].
• This finding is confirmed by sequences around the C. glabrata TRP1 and IPP1 loci, which show that it contains sister regions derived from the same duplication event as that of S. cerevisiae [8].
• Here, we describe the generation of a conditional S. cerevisiae mutant (named YPC-1) whose functional IPP1 gene is under the control of a galactose-dependent promoter [9].
• During the rapid exchange of oxygens of Pi with water catalyzed by yeast inorganic pyrophosphatase, Pi at the catalytic site may either dissociate or undergo reversible loss of an oxygen to water [10].

Chemical compound and disease context of IPP1

• The enzyme.PP(i) intermediate formed during PP(i) hydrolysis binds fluoride much faster (yeast PPase) or tighter (E. coli PPase) than the similar complex existing at equilibrium with P(i) [1].
• Tightly bound pyrophosphate in Escherichia coli inorganic pyrophosphatase [11].

Biological context of IPP1

• Using gene disruptions, we found that PPA1 is required for cell growth [12].
• The present paper describes the amino acid sequence analysis of the internal and COOH-terminal cyanogen bromide fragments of yeast inorganic pyrophosphatase (Sterner, R., Noyes, C., and Heinrikson, R.L. (1974) Biochemistry 13, 91-99) [13].
• The PPA gene appears to be present in a single copy within the S. cerevisiae genome and has been localized to chromosome II [14].
• Nucleotide sequence of S. pombe inorganic pyrophosphatase [15].
• The R78K and D117E active-site variants of Saccharomyces cerevisiae soluble inorganic pyrophosphatase: structural studies and mechanistic implications [16].

Anatomical context of IPP1

• Evidence for a membrane potential (delta psi) generating capacity of inorganic pyrophosphate (PPi) with inorganic pyrophosphatase in mitochondria from the yeast Saccharomyces cerevisiae is presented [17].
• Properties of inorganic pyrophosphatase of pig scapula cartilage [18].
• H(+)-translocating inorganic pyrophosphatase of plant vacuoles. Inhibition by Ca2+, stabilization by Mg2+ and immunological comparison with other inorganic pyrophosphatases [19].
• When the water activity of the medium is reduced by the addition of organic solvents, soluble yeast inorganic pyrophosphatase (no H+ gradient present) synthesizes pyrophosphate in amounts similar to those synthesized by the chromatophores in totally aqueous medium during illumination, (H+ gradient present) [20].

Associations of IPP1 with chemical compounds

• We have developed two methods for quantitatively measuring inorganic pyrophosphate (PPi) in the presence of 10(3)--10(4) molar excesses of inorganic phosphate (Pi) and used them to measure the extent of enzyme-bound pyrophosphate (EPPi) formation in solutions of yeast inorganic pyrophosphatase and Pi [21].
• The fluoride ion is a potent and specific inhibitor of cytoplasmic pyrophosphatase (PPase) [1].
• These two results provide strong evidence for the conclusion that PPase catalyzes inorganic pyrophosphate hydrolysis via a single-step direct phosphoryl transfer to water and does not involve formation of a phosphorylated enzyme intermediate [22].
• The regiospecificity and stereospecificity of proton transfer in the yeast inorganic pyrophosphatase (PPase) catalyzed hydrolysis of P1,P2-bidentate Mg(H2O)4(PPi)2- were probed with exchange-inert metal complexes of imidodiphosphate (PNP) and thiopyrophosphate (PPS) [23].
• Identification of an arginine important for enzymatic activity within the covalent structure of yeast inorganic pyrophosphatase [24].

Other interactions of IPP1

• Yeast PPA2 gene encodes a mitochondrial inorganic pyrophosphatase that is essential for mitochondrial function [12].
• The syntheses used pyruvate kinase, UDP-Glc pyrophosphorylase, and inorganic pyrophosphatase, and the regenerated UDP-Glc was cycled approximately 10 times [25].

Analytical, diagnostic and therapeutic context of IPP1

• Molecular cloning and functional expression of cDNA encoding a mammalian inorganic pyrophosphatase [26].
• A segment of DNA encoding Saccharomyces cerevisiae inorganic pyrophosphatase (ppa gene) was amplified by the polymerase chain reaction [27].
• Amino acid analysis and sequence analysis of the peptide revealed that it comprised residues 96-119 of the inorganic pyrophosphatase from thermophilic bacterium PS-3 [28].
• Hexameric inorganic pyrophosphatase of Escherichia coli contains about 1 mol/mol of 'structural' pyrophosphate, which survives gel filtration and prolonged incubation with Mg2+, does not exchange with medium phosphate and pyrophosphate but is removed with 0.8 M perchloric acid [11].
• Trace [32P] gamma ATP was added at the start of the infusion; conversion to [32P] Pi and to [32P] PPi was determined by precipitation of Pi as reduced phosphomolybdate before and after treatment with yeast inorganic pyrophosphatase [29].

References