This domain is found at the N-terminal of strictosidine synthase-like (SSL) proteins including Adipocyte plasma membrane- associated proteins (APMAPs) from animals, Protein STRICTOSIDINE SYNTHASE-LIKE (SSLs) from Arabidopsis and SGL proteins, being also present in bacterial sequences. It is about 50 amino acids in length. It contains residues involved in metal coordination in the active site. This domain is also found in Gluconolactonase and Sugar lactone lactonase. These proteins share a six-bladed beta-propeller fold structure and have similar structural and mechanistic features to SS (strictosidine synthase) that involve nucleophilic attack on an electrophilic substrate, although they do not catalyse the SS reaction as they lack the catalytic glutamate required for SS activity; they catalyse hydrolytic reactions instead [1,2,3,4]. APMAPs shows similarity with paraoxonases (PON) and has a strong arylesterase activity with beta-naphthyl acetate and phenyl acetate. They are involved in adipocyte differentiation [1,3]. [1]. 18513186. Localization and characterization of the novel protein encoded by C20orf3. Ilhan A, Gartner W, Nabokikh A, Daneva T, Majdic O, Cohen G, Bohmig GA, Base W, Horl WH, Wagner L;. Biochem J. 2008;414:485-495. [2]. 18280746. 3D-Structure and function of strictosidine synthase--the key enzyme of monoterpenoid indole alkaloid biosynthesis. Stockigt J, Barleben L, Panjikar S, Loris EA;. Plant Physiol Biochem. 2008;46:340-355. [3]. 21948213. The evolution of function in strictosidine synthase-like proteins. Hicks MA, Barber AE 2nd, Giddings LA, Caldwell J, O'Connor SE, Babbitt PC;. Proteins. 2011;79:3082. TRUNCATED at 1650 bytes (from Pfam)
- Date:
- 2024-10-16