Bacillus subtilis ORF yybQ encodes a manganese-dependent inorganic pyrophosphatase with distinctive properties: the first of a new class of soluble pyrophosphatase?

Young, Tom; Kuhn, Nicholas J.; Wadeson, Albert; Ward, Simon; Burges, Dan; Cooke, George Dunstan

doi:10.1099/00221287-144-9-2563

Cited by 92 publications

(92 citation statements)

References 58 publications

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“…Family II of Soluble PPases-A new family of soluble PPases (family II) has recently been observed by two research groups (10,11). The first verified member of family II PPases was B. subtilis PPase, but in addition, amino acid sequences of four putative members of this family were found in the GenBank TM , two streptococcal and two archeal (11).…”

Section: Discussionmentioning

confidence: 99%

“…Another unique property of B. subtilis PPase is its preference for Mn 2ϩ over Mg 2ϩ as the activator. A search through GenBank TM revealed four more putative prokaryotic members of family II (two streptococcal and two archeal), showing 40 -57% identity in amino acid sequence (10,11). One of them (from Methanococcus jannaschii) has been recently cloned and expressed in E. coli (13).…”

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confidence: 99%

“…Recently, a long-known PPase of Bacillus subtilis (9) was found to have a completely different amino acid sequence and therefore to belong to a different family (family II) of soluble PPases (10,11). B. subtilis PPase is similar to family I PPases in requiring divalent metal ions for activity (9), but unlike bacterial family I PPases, it is formed by large subunits (34 kDa) and displays 10 -20 times greater activity (9,12).…”

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confidence: 99%

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Quaternary Structure and Metal Ion Requirement of Family II Pyrophosphatases from Bacillus subtilis,Streptococcus gordonii, and Streptococcus mutans

Parfenyev

Salminen

Halonen

et al. 2001

Journal of Biological Chemistry

137

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Pyrophosphatase (PPase) from Bacillus subtilis has recently been found to be the first example of a family II soluble PPase with a unique requirement for Mn 2؉ . In the present work, we cloned and overexpressed in Escherichia coli putative genes for two more family II PPases (from Streptococcus mutans and Streptococcus gordonii), isolated the recombinant proteins, and showed them to be highly specific and active PPases (catalytic constants of 1700 -3300 s ؊1 at 25°C in comparison with 200 -400 s ؊1 for family I). All three family II PPases were found to be dimeric manganese metalloenzymes, dissociating into much less active monomers upon removal of Mn 2؉ . The dimers were found to have one high affinity manganese-specific site (K d of 0.2-3 nM for Mn 2؉ and 10 -80 M for Mg 2؉ ) and two or three moderate affinity sites (K d ϳ 1 mM for both cations) per subunit. Mn 2؉ binding to the high affinity site, which occurs with a half-time of less than 10 s at 1.5 mM Mn 2؉ , dramatically shifts the monomer 7 dimer equilibrium in the direction of the dimer, further activates the dimer, and allows substantial activity (60 -180 s ؊1 ) against calcium pyrophosphate, a potent inhibitor of family I PPases.

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Section: Discussionmentioning

confidence: 99%

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Quaternary Structure and Metal Ion Requirement of Family II Pyrophosphatases from Bacillus subtilis,Streptococcus gordonii, and Streptococcus mutans

Parfenyev

Salminen

Halonen

et al. 2001

Journal of Biological Chemistry

137

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“…Pyrophosphatase (EC 3.6.1.1) favors the former reaction by effectively removing inorganic pyrophosphates (PP i ) to phosphates (6). Soluble pyrophosphatases from a wide variety of sources have been identified and classified to two superfamilies, the inorganic pyrophosphatase superfamily (family I) and the DHH (Asp-His-His) phosphoesterase superfamily (family II) (5,29,32). However, a specific enzyme for the reaction has not been pinpointed yet.…”

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Identification and Characterization of Inorganic Pyrophosphatase and PAP Phosphatase from Thermococcus onnurineus NA1

et al. 2009

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Two hypothetical genes were functionally verified to be a pyrophosphatase and a PAP phosphatase in Thermococcus onnurineus NA1. This is the first report of the pyrophosphatases and the PAP phosphatases being organized in the gene clusters of the sulfate activation system only in T. onnurineus NA1 and "Pyrococcus abyssi."Sulfate is assimilated through reduction to sulfite and incorporation into the sulfur metabolites such as cysteine, methionine, or homocysteine (4) and through sulfation of various metabolites by the action of sulfotransferases (13,15,22,27) (Fig. 1). The sulfate assimilation pathways require the activation of sulfate, forming adenosine 5Ј-phosphosulfate (APS) by ATP-sulfurylase (EC 2.7.7.4) and 3Ј-phosphoadenosine-5Ј-phosphosulfate (PAPS) by APS kinase (EC 2.7

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“…There are several categories of PPases, of which soluble PPases identified from prokaryote, yeast, plant and mammalian tissues, have been classified into Family I and Family II PPases to date. The two families of PPases, however, have no sequence similarity at amino acid level and have distinct catalytic features [10,13,14,19]. Among the Family I PPases, the most well characterized PPases are those from E. coli [8,12] and yeast [4,11,15].…”

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Temperature and Metal Ions-Dependent Activity of the Family I Inorganic Pyrophosphatase from the Swine Roundworm Ascaris suum

Islam

Miyoshi

Isobe

et al. 2004

The Journal of Veterinary Medical Science

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ABSTRACT. Temperature dependence, heat stability and metal ions-dependent activity were examined on the Family I inorganic pyrophosphatase (PPase) recently identified from Ascaris suum. Recombinant A. suum PPase (rAsPPase) showed an optimal activity at 55°C. The rAsPPase was heat stable at 40°C in the absence of added Mg 2+ and at 50°C in its presence. The enzyme required divalent metal ions for its activity. The preferences for the metal ions (5 mM concentration) were in the order: Mg 2+ > Co 2+ > Cu 2+ > Fe 2+ > Zn 2+ >Mn 2+ . On the contrary, enzyme activity was inhibited by Ca 2+ . These findings suggest that catalytic features of AsPPase are consistent with the Family I PPases reported from a wide range of organisms. KEY WORDS: Ascaris suum, enzyme activity, Family I inorganic pyrophosphatase.J. Vet. Med. Sci. 66(2): 221-223, 2004 Inorganic pyrophosphatase (PPase, EC 3.6.1.1) is an important enzyme that hydrolyzes inorganic pyrophosphate (PP i ) to produce 2 inorganic ortho-phosphates (P i ). The major role of PPase is to control the level of PP i which have been continuously produced as a result of biosynthesis of macromolecular compounds in the living cell. The enzyme is shown to be essential for life [3,9]. There are several categories of PPases, of which soluble PPases identified from prokaryote, yeast, plant and mammalian tissues, have been classified into Family I and Family II PPases to date. The two families of PPases, however, have no sequence similarity at amino acid level and have distinct catalytic features [10,13,14,19]. Among the Family I PPases, the most well characterized PPases are those from E. coli [8,12] and yeast [4,11,15]. The enzymes have shown strong metal iondependency, with Mg 2+ conferring the highest PP i -hydrolysis activity [4], and sensitive to inhibition by Ca 2+ [17].Recently, we cloned and characterized a gene that encodes a functional Family I PPase of the swine roundworm A. suum [7]. The A. suum PPase (AsPPase) has a molecular mass of 40 kDa and a pI of 7.1, and its homologs were expressed in human and dog roundworms, A. lumbricoides and Toxocara canis respectively. The enzymes were intensely localized under the hypodermis of adult worm. Interestingly, we demonstrated a novel role of PPase enzyme in the development and molting process of A. suum third-stage larvae to fourth-stage in vitro. It is therefore of interest to investigate into the enzymatic properties of molting-associated AsPPase in some details. In this study, we determined temperature dependence, heat stability and divalent metal ions-dependent activity of A. suum PPase enzyme to provide insight into the PPase-regulated roundworm metabolism and/or optimum growth and survival.Recombinant AsPPase with a specific activity of 937 µmol P i /min/mg of protein was used in the present study. Enzyme activity was determined spectrophotometrically using a molybdate-blue based colorimetric assay as previously described [7]. Enzyme (specific) activity was defined as µmol of P i liberated by the hydrolysis of PP i per m...

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Bacillus subtilis ORF yybQ encodes a manganese-dependent inorganic pyrophosphatase with distinctive properties: the first of a new class of soluble pyrophosphatase?

Cited by 92 publications

References 58 publications

Quaternary Structure and Metal Ion Requirement of Family II Pyrophosphatases from Bacillus subtilis,Streptococcus gordonii, and Streptococcus mutans

Quaternary Structure and Metal Ion Requirement of Family II Pyrophosphatases from Bacillus subtilis,Streptococcus gordonii, and Streptococcus mutans

Identification and Characterization of Inorganic Pyrophosphatase and PAP Phosphatase from Thermococcus onnurineus NA1

Temperature and Metal Ions-Dependent Activity of the Family I Inorganic Pyrophosphatase from the Swine Roundworm Ascaris suum

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