Group of proteins having inorganic pyrophosphatase activity
inorganic pyrophosphatase
Pyrophosphatase (inorganic) hexamer, E.Coli
Identifiers
EC no.
3.6.1.1
CAS no.
9024-82-2
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BRENDA
BRENDA entry
ExPASy
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KEGG
KEGG entry
MetaCyc
metabolic pathway
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proteins
Soluble inorganic pyrophosphatase
Structure of soluble inorganic pyrophosphatase, isolated from Thermococcus litoralis (PDB: 2PRD).
Identifiers
Symbol
Pyrophosphatase
Pfam
PF00719
InterPro
IPR008162
PROSITE
PS00387
CATH
2prd
SCOP2
2prd / SCOPe / SUPFAM
CDD
cd00412
Available protein structures:
Pfam
structures / ECOD
PDB
RCSB PDB; PDBe; PDBj
PDBsum
structure summary
pyrophosphatase (inorganic) 1
Identifiers
Symbol
PPA1
Alt. symbols
PP
NCBI gene
5464
HGNC
9226
OMIM
179030
RefSeq
NM_021129
UniProt
Q15181
Other data
Locus
Chr. 10 q11.1-q24
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pyrophosphatase (inorganic) 2
Identifiers
Symbol
PPA2
NCBI gene
27068
HGNC
28883
OMIM
609988
RefSeq
NM_176869
UniProt
Q9H2U2
Other data
Locus
Chr. 4 q25
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Inorganic pyrophosphatase (or inorganic diphosphatase, PPase) is an enzyme (EC 3.6.1.1) that catalyzes the conversion of one ion of pyrophosphate to two phosphate ions.[1] This is a highly exergonic reaction, and therefore can be coupled to unfavorable biochemical transformations in order to drive these transformations to completion.[2] The functionality of this enzyme plays a critical role in lipid metabolism (including lipid synthesis and degradation), calcium absorption and bone formation,[3][4] and DNA synthesis,[5] as well as other biochemical transformations.[6][7]
Two types of inorganic diphosphatase, very different in terms of both amino acid sequence and structure, have been characterised to date: soluble and transmembrane proton-pumping pyrophosphatases (sPPases and H(+)-PPases, respectively). sPPases are ubiquitous proteins that hydrolyse pyrophosphate to release heat, whereas H+-PPases, so far unidentified in animal and fungal cells, couple the energy of PPi hydrolysis to proton movement across biological membranes.[8][9]
^Harold FM (December 1966). "Inorganic polyphosphates in biology: structure, metabolism, and function". Bacteriological Reviews. 30 (4): 772–94. doi:10.1128/MMBR.30.4.772-794.1966. PMC 441015. PMID 5342521.
^Terkeltaub RA (July 2001). "Inorganic pyrophosphate generation and disposition in pathophysiology". American Journal of Physiology. Cell Physiology. 281 (1): C1–C11. doi:10.1152/ajpcell.2001.281.1.C1. PMID 11401820.
^Orimo H, Ohata M, Fujita T (September 1971). "Role of inorganic pyrophosphatase in the mechanism of action of parathyroid hormone and calcitonin". Endocrinology. 89 (3): 852–8. doi:10.1210/endo-89-3-852. PMID 4327778.
^Poole KE, Reeve J (December 2005). "Parathyroid hormone - a bone anabolic and catabolic agent". Current Opinion in Pharmacology. 5 (6): 612–7. doi:10.1016/j.coph.2005.07.004. PMID 16181808.
^Nelson, David L.; Cox, Michael M. (2000). Lehninger Principles of Biochemistry, 3rd ed. New York: Worth Publishers. pp. 937. ISBN 1-57259-153-6.
^Ko KM, Lee W, Yu JR, Ahnn J (November 2007). "PYP-1, inorganic pyrophosphatase, is required for larval development and intestinal function in C. elegans". FEBS Letters. 581 (28): 5445–53. doi:10.1016/j.febslet.2007.10.047. PMID 17981157. S2CID 40325661.
^Usui Y, Uematsu T, Uchihashi T, Takahashi M, Takahashi M, Ishizuka M, et al. (May 2010). "Inorganic polyphosphate induces osteoblastic differentiation". Journal of Dental Research. 89 (5): 504–9. doi:10.1177/0022034510363096. PMID 20332330. S2CID 44916855.
^Perez-Castineira JR, Lopez-Marques RL, Villalba JM, Losada M, Serrano A (December 2002). "Functional complementation of yeast cytosolic pyrophosphatase by bacterial and plant H+-translocating pyrophosphatases". Proc. Natl. Acad. Sci. U.S.A. 99 (25): 15914–9. Bibcode:2002PNAS...9915914P. doi:10.1073/pnas.242625399. hdl:11441/26079. PMC 138539. PMID 12451180.
^Baltscheffsky M, Schultz A, Baltscheffsky H (September 1999). "H+ -PPases: a tightly membrane-bound family". FEBS Lett. 457 (3): 527–33. doi:10.1016/S0014-5793(99)90617-8. PMID 10523139. S2CID 12452334.
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Udagawa N, Fukasawa K, Hiraoka BY, Mogi M (February 1986). "Inorganicpyrophosphatase activity of purified bovine pulp alkaline phosphatase at physiological...
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