3'(2'),5'-bisphosphate nucleotidase

The enzyme 3′(2′),5′-bisphosphate nucleotidase (EC 3.1.3.7) catalyzes the reaction

adenosine 3′,5′-bisphosphate + H2O

    ⇌
  

{\displaystyle \rightleftharpoons }

AMP + phosphate

This enzyme belongs to the family of hydrolases, specifically those acting on phosphoric monoester bonds. The systematic name is adenosine-3′(2′),5′-bisphosphate 3′(2′)-phosphohydrolase. Other names in common use include phosphoadenylate 3′-nucleotidase, 3′-phosphoadenylylsulfate 3′-phosphatase, and 3′(2′),5′-bisphosphonucleoside 3′(2′)-phosphohydrolase. This enzyme participates in sulfur metabolism.

As of late 2007, 6 structures have been solved for this class of enzymes, with PDB accession codes 1JP4, 1K9Y, 1K9Z, 1KA0, 1KA1, and 1QGX.

• .mw-parser-output cite.citation{font-style:inherit;word-wrap:break-word}.mw-parser-output .citation q{quotes:"""""""'""'"}.mw-parser-output .citation:target{background-color:rgba(0,127,255,0.133)}.mw-parser-output .id-lock-free.id-lock-free a{background:url("//upload.wikimedia.org/wikipedia/commons/6/65/Lock-green.svg")right 0.1em center/9px no-repeat}.mw-parser-output .id-lock-limited.id-lock-limited a,.mw-parser-output .id-lock-registration.id-lock-registration a{background:url("//upload.wikimedia.org/wikipedia/commons/d/d6/Lock-gray-alt-2.svg")right 0.1em center/9px no-repeat}.mw-parser-output .id-lock-subscription.id-lock-subscription a{background:url("//upload.wikimedia.org/wikipedia/commons/a/aa/Lock-red-alt-2.svg")right 0.1em center/9px no-repeat}.mw-parser-output .cs1-ws-icon a{background:url("//upload.wikimedia.org/wikipedia/commons/4/4c/Wikisource-logo.svg")right 0.1em center/12px no-repeat}body:not(.skin-timeless):not(.skin-minerva) .mw-parser-output .id-lock-free a,body:not(.skin-timeless):not(.skin-minerva) .mw-parser-output .id-lock-limited a,body:not(.skin-timeless):not(.skin-minerva) .mw-parser-output .id-lock-registration a,body:not(.skin-timeless):not(.skin-minerva) .mw-parser-output .id-lock-subscription a,body:not(.skin-timeless):not(.skin-minerva) .mw-parser-output .cs1-ws-icon a{background-size:contain;padding:0 1em 0 0}.mw-parser-output .cs1-code{color:inherit;background:inherit;border:none;padding:inherit}.mw-parser-output .cs1-hidden-error{display:none;color:var(--color-error,#bf3c2c)}.mw-parser-output .cs1-visible-error{color:var(--color-error,#bf3c2c)}.mw-parser-output .cs1-maint{display:none;color:#085;margin-left:0.3em}.mw-parser-output .cs1-kern-left{padding-left:0.2em}.mw-parser-output .cs1-kern-right{padding-right:0.2em}.mw-parser-output .citation .mw-selflink{font-weight:inherit}@media screen{.mw-parser-output .cs1-format{font-size:95%}html.skin-theme-clientpref-night .mw-parser-output .cs1-maint{color:#18911f}}@media screen and (prefers-color-scheme:dark){html.skin-theme-clientpref-os .mw-parser-output .cs1-maint{color:#18911f}}Brungraber EG (1958). "Nucleotides involved in the enzymatic conjugation of phenols with sulfate". J. Biol. Chem. 233 (2): 472–477. doi:10.1016/S0021-9258(18)64786-6. PMID 13563523.
• Farooqui AA, Balasubramanian AS (1970). "Enzymatic dephosphorylation 3′-phosphoadenosine 5′-phoaphosulfate to adenosine 5′-phosphosulfate in sheep brain". Biochim. Biophys. Acta. 198 (1): 56–65. doi:10.1016/0005-2744(70)90032-x. PMID 4313079.
• Ramaswamy SG, Jakoby WB (1987). "(2′)3′,5′-Bisphosphate nucleotidase". J. Biol. Chem. 262 (21): 10044–7. doi:10.1016/S0021-9258(18)61072-5. PMID 3038862.
• Lik-Shing Tsang M, Schiff JA (1976). "Properties of enzyme fraction A from Chlorella and copurification of 3′(2′),5′-biphosphonucleoside 3′(2′)-phosphohydrolase, adenosine 5′phosphosulfate sulfohydrolase and adenosine-5′-phosphosulfate cyclase activities". Eur. J. Biochem. 65 (1): 113–21. doi:10.1111/j.1432-1033.1976.tb10395.x. PMID 179817.