4rgy

</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4rgy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4rgy OCA], [https://pdbe.org/4rgy PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4rgy RCSB], [https://www.ebi.ac.uk/pdbsum/4rgy PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4rgy ProSAT]</span></td></tr>

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== Publication Abstract from PubMed ==

A low-temperature-active alkaline esterase, Est12, from a marine sediment metagenomic fosmid library was identified. Est12 prefers short- and middle-chain p-nitrophenol esters as substrate with optimum temperature and pH value of 50 degrees C and 9.0, respectively, and nearly 50 % of maximum activity retained at 5 degrees C. The hydrolysis activity of Est12 was stable at 40 degrees C. Ca2+ especially activated the activity of Est12 to about 151 % of the control. DEPC and PMSF inhibited the activity of Est12 to 34 and 25 %, respectively. In addition, Est12 was more tolerable to methanol compared to other organic solvents tested. The crystal structure of Est12 at 1.39 A resolution showed that the cap domain which is composed of an alpha-helix and a flexible region resulted in a relatively wide spectrum of substrate, with p-nitrophenol caproate as the preferred one. Furthermore, the flexible cap domain and the high percentage of Gly, Ser, and Met may play important roles in the adaptation of Est12 to low temperature.

Structural and functional analysis of a low-temperature-active alkaline esterase from South China Sea marine sediment microbial metagenomic library.,Hu Y, Liu Y, Li J, Feng Y, Lu N, Zhu B, Xue S J Ind Microbiol Biotechnol. 2015 Sep 8. PMID:26350078<ref>PMID:26350078</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>

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== References ==

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