Acid phosphatase: Difference between revisions
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'''Acid phosphatase''' (ACP, EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.3.2 3.1.3.2]) is an enzyme which removes phosphate from other molecules during digestion. It catalyzes the conversion of orthophosphoric monoester and H<sub>2</sub>O to alcohol and phosphoric acid. The enzyme is most effective in acidic environment, hence its name.<ref>PMID:11950951</ref><br /> | '''Acid phosphatase''' (ACP, EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.3.2 3.1.3.2]) is an enzyme which removes phosphate from other molecules during digestion. It catalyzes the conversion of orthophosphoric monoester and H<sub>2</sub>O to alcohol and phosphoric acid. The enzyme is most effective in acidic environment, hence its name.<ref>PMID:11950951</ref><br /> | ||
*'''Prostatic ACP''' (PSAP) is produced by the prostate<ref>PMID:20645695</ref>.<br /> | *'''Prostatic ACP''' (PSAP) is produced by the prostate<ref>PMID:20645695</ref>.<br /> | ||
*'''Purple ACP''' (PAP) or '''tartrate-resistant ACP''' contains a dinuclear Fe center and their oxidized form in solution maintains a purple color. <br /> | *'''Purple ACP''' (PAP) or '''tartrate-resistant ACP''' contains a dinuclear Fe center and their oxidized form in solution maintains a purple color<ref>PMID:34402946</ref>. <br /> | ||
*'''Histidine ACP''' (HAP) catalyzes the transfer of phosphoryl group using an active-site histidine.<br /> | *'''Histidine ACP''' (HAP) catalyzes the transfer of phosphoryl group using an active-site histidine<ref>PMID:18092946</ref> | ||
*''' | *'''N-acetylneuraminic ACP''' is involved in the biosynthesis of N-acetylneuraminate.<br /> | ||
*'''Lysophosphatidic ACP''' is involved in signal transduction and storage lipid synthesis<ref>PMID:20045079</ref>.<br /> | |||
BA42 belongs to the TPM protein family from Pfam. The TPM domain family is named after the three founding proteins TLP18.3, Psb32 and MOLO-1. TPM domains have a characteristic fold <scene name='71/715464/Cv/2'>(αβαβαββαα or βαβαββαα)</scene> composed of α helices (3+3<ref>pmid 21908686</ref> or 2+3<ref>pmid 22198206</ref>) flanking four central β strands. The TPM fold has not been found in other protein domains to date. TPM was previously referred to as "DUF477" and "Repair_PSII". | *'''BA42''' belongs to the TPM protein family from Pfam. The TPM domain family is named after the three founding proteins TLP18.3, Psb32 and MOLO-1. TPM domains have a characteristic fold <scene name='71/715464/Cv/2'>(αβαβαββαα or βαβαββαα)</scene> composed of α helices (3+3<ref>pmid 21908686</ref> or 2+3<ref>pmid 22198206</ref>) flanking four central β strands. The TPM fold has not been found in other protein domains to date. TPM was previously referred to as "DUF477" and "Repair_PSII". | ||
ACP contains 3 classes:<br /> | ACP contains 3 classes:<br /> | ||
