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Alpha/beta hydrolase fold
The alpha/beta hydrolase fold[1] is common to a number of hydrolytic enzymes of widely differing phylogenetic origin and catalytic function. The core of each enzyme is a alpha/beta-sheet (rather than a barrel), containing 8 strands connected by helices[1]. The enzymes are believed to have diverged from a common ancestor, preserving the arrangement of the catalytic residues. All have a catalytic triad, the elements of which are borne on loops, which are the best conserved structural features of the fold. Additional recommended knowledgeThis catalytic domain is found in a very wide range of enzymes. Subfamilies
Human proteins containing this domainABHD10; ABHD11; ABHD12; ABHD12B; ABHD13; ABHD2; ABHD3; ABHD4; ABHD5; ABHD6; ABHD7; ABHD8; ABHD9; BAT5; BPHL; C20orf135; EPHX1; EPHX2; FAM108B1; LIPA; LIPF; LIPJ; LIPK; LIPM; LIPN; MEST; MGLL; PPME1; SERHL; SERHL2; SPG21; Categories: Protein domains | Peripheral membrane proteins | Hydrolases |
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This article is licensed under the GNU Free Documentation License. It uses material from the Wikipedia article "Alpha/beta_hydrolase_fold". A list of authors is available in Wikipedia. |