Balance puzzle - Revision history

212.74.97.205: /* Solution */

2014-06-18T13:46:09Z

Solution

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	~~\| Name = Diphosphoinositol-polyphosphate diphosphatase~~
	~~\| EC_number = 3~~.6.1.52
	~~\| CAS_number =~~
	~~\| IUBMB_EC_number = 3~~/6/1/52
	~~\| GO_code =~~
	~~\| image =~~
	~~\| width =~~
	~~\| caption =~~
	}}
	~~In [[enzymology]~~], a ~~'''diphosphoinositol~~-~~polyphosphate diphosphatase~~'~~'' ({{EC number\|3~~.6.1.~~52}})~~ is ~~an [[enzyme]] that [[catalysis\|catalyzes]]~~ the ~~[[chemical reaction]]~~

	~~:diphospho~~-~~myo~~-~~inositol polyphosphate + H~~<~~sub~~>2<~~/sub~~>O <~~math~~>~~\rightleftharpoons~~<~~/math~~> ~~myo-inositol polyphosphate + phosphate~~

	~~Thus~~, the ~~two~~ [~~[substrate (biochemistry)\|substrates]~~] of this ~~enzyme~~ are ~~[[diphospho-myo-inositol polyphosphate]] and [[water\|H~~<~~sub~~>2<~~/sub~~>~~O]], whereas its two [[product (chemistry)\|products]] are [[myo-inositol polyphosphate]]~~ and ~~[[phosphate]]~~.

	~~This enzyme belongs~~ to ~~the family~~ of ~~[[hydrolase]]s~~, ~~specifically those acting on acid anhydrides in phosphorus-containing anhydrides~~. ~~The systematic name of this enzyme class~~ is ~~'''diphospho-myo-inositol-polyphosphate diphosphohydrolase'''~~. ~~Other names in common use include '''diphosphoinositol-polyphosphate phosphohydrolase''',~~ and ~~'''DIPP'''~~.

	~~==Structural studies==~~

	As of ~~late 2007~~, 3 [~~[tertiary structure\|structures]~~] have ~~been solved for this class~~ of ~~enzymes~~, ~~with~~ [~~[Protein Data Bank\|PDB~~]~~] accession codes {{PDB link\|2DUK}}, {{PDB link\|2FVV}},~~ and ~~{{PDB link\|2Q9P}}~~.

	~~==References==~~
	~~{{reflist\|1}}~~
	* {{cite journal \| author = Shears SB \| year = 1998 \| title = A ~~novel context~~ for ~~the 'MutT' module~~, ~~a guardian~~ of ~~cell integrity~~, in a ~~diphosphoinositol polyphosphate phosphohydrolase \| journal = EMBO J~~. ~~\| volume = 17 \| pages = 6599–607 \| pmid = 9822604 \| doi = 10~~.~~1093/emboj/17~~.22.6599 \| last2 = Caffrey \| first2 = JJ \| last3 = Yang \| first3 = X \| last4 = Bembenek \| first4 = ME \| last5 = Moyer \| first5 = MB \| last6 = Burkhart \| first6 = WA \| last7 = Shears \| first7 = SB \| issue = 22 \| pmc = 1171006 }}
	* {{cite journal \| author = Caffrey JJ, ~~Safrany ST~~, ~~Yang X~~, ~~Shears SB \| year = 2000 \| title = Discovery of molecular~~ and ~~catalytic diversity among human diphosphoinositol-polyphosphate phosphohydrolases~~. ~~An expanding Nudt family \| journal = J~~. ~~Biol~~. ~~Chem. \| volume~~ = ~~275 \| pages~~ = ~~12730~~&~~ndash;6 \| pmid~~ = ~~10777568 \| doi~~ = ~~10.1074/jbc~~.~~275.17.12730 \| issue = 17 }}~~

	~~[[Category:EC 3.6.1]]~~
	~~[[Category:Enzymes of known structure]]~~


	~~{{hydrolase-stub}}~~

en>WikiDan61: Fixed the single citation. Tagged for needing more.

2014-01-14T15:06:48Z

Fixed the single citation. Tagged for needing more.

← Older revision		Revision as of 17:06, 14 January 2014
Line 1:		Line 1:
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			\| Name = Diphosphoinositol-polyphosphate diphosphatase
			\| EC_number = 3.6.1.52
			\| CAS_number =
			\| IUBMB_EC_number = 3/6/1/52
			\| GO_code =
			\| image =
			\| width =
			\| caption =
			}}
			In [[enzymology]], a '''diphosphoinositol-polyphosphate diphosphatase''' ({{EC number\|3.6.1.52}}) is an [[enzyme]] that [[catalysis\|catalyzes]] the [[chemical reaction]]

			:diphospho-myo-inositol polyphosphate + H<sub>2</sub>O <math>\rightleftharpoons</math> myo-inositol polyphosphate + phosphate

			Thus, the two [[substrate (biochemistry)\|substrates]] of this enzyme are [[diphospho-myo-inositol polyphosphate]] and [[water\|H<sub>2</sub>O]], whereas its two [[product (chemistry)\|products]] are [[myo-inositol polyphosphate]] and [[phosphate]].

			This enzyme belongs to the family of [[hydrolase]]s, specifically those acting on acid anhydrides in phosphorus-containing anhydrides. The systematic name of this enzyme class is '''diphospho-myo-inositol-polyphosphate diphosphohydrolase'''. Other names in common use include '''diphosphoinositol-polyphosphate phosphohydrolase''', and '''DIPP'''.

			==Structural studies==

			As of late 2007, 3 [[tertiary structure\|structures]] have been solved for this class of enzymes, with [[Protein Data Bank\|PDB]] accession codes {{PDB link\|2DUK}}, {{PDB link\|2FVV}}, and {{PDB link\|2Q9P}}.

			==References==
			{{reflist\|1}}
			* {{cite journal \| author = Shears SB \| year = 1998 \| title = A novel context for the 'MutT' module, a guardian of cell integrity, in a diphosphoinositol polyphosphate phosphohydrolase \| journal = EMBO J. \| volume = 17 \| pages = 6599–607 \| pmid = 9822604 \| doi = 10.1093/emboj/17.22.6599 \| last2 = Caffrey \| first2 = JJ \| last3 = Yang \| first3 = X \| last4 = Bembenek \| first4 = ME \| last5 = Moyer \| first5 = MB \| last6 = Burkhart \| first6 = WA \| last7 = Shears \| first7 = SB \| issue = 22 \| pmc = 1171006 }}
			* {{cite journal \| author = Caffrey JJ, Safrany ST, Yang X, Shears SB \| year = 2000 \| title = Discovery of molecular and catalytic diversity among human diphosphoinositol-polyphosphate phosphohydrolases. An expanding Nudt family \| journal = J. Biol. Chem. \| volume = 275 \| pages = 12730–6 \| pmid = 10777568 \| doi = 10.1074/jbc.275.17.12730 \| issue = 17 }}

			[[Category:EC 3.6.1]]
			[[Category:Enzymes of known structure]]


			{{hydrolase-stub}}

en>Thorvaldurgunn: Undid revision 491500083 by 97.102.152.232 (talk)

2012-06-05T10:44:51Z

Undid revision 491500083 by 97.102.152.232 (talk)

New page

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