Acid phosphatase: Difference between revisions
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*'''Histidine ACP''' (HAP) catalyzes the transfer of phosphoryl group using an active-site histidine<ref>PMID:18092946</ref> | *'''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 /> | *'''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". | ||