مورد إلكتروني

Coupling of the i-face and the active site of phospholipase A2 for interfacial activation.

التفاصيل البيبلوغرافية
العنوان: Coupling of the i-face and the active site of phospholipase A2 for interfacial activation.
بيانات النشر: Molekylär evolution 2006
تفاصيل مُضافة: Jain, Mahendra Kumar
Berg, Otto G.
نوع الوثيقة: Electronic Resource
مستخلص: Interfacial enzymes bind to organized interfaces where they access their substrates. As an example of interfacial activation, phospholipase A2 has an observed rate of hydrolysis of the sn-2-acyl chain of phospholipids at bilayer and micellar interfaces that is more than 1,000 times larger than with monodisperse phospholipids. The major challenge for the study of interfacial enzymes is to correlate the elementary steps of the interfacial function of the enzyme with the structure of the enzyme at the interface. Having kinetically resolved the steps of the interfacial turnover cycle, here we outline our recent (mostly since 2000) approaches to address remaining issues of interfacial activation and also the protocols that are likely to provide insights into the distinguishing structural features of the interface-activated enzyme.
مصطلحات الفهرس: Animals, Binding Sites, Enzyme Activation/physiology, Hydrolysis, Kinetics, Models; Molecular, Pancreas/enzymology, Phospholipases A/*chemistry, Phospholipids/chemistry, Surface Properties, Swine, Biochemistry and Molecular Biology, Biokemi och molekylärbiologi, Article in journal, info:eu-repo/semantics/article, text
DOI: 10.1016.j.cbpa.2006.08.015
URL: http://urn.kb.se/resolve?urn=urn:nbn:se:uu:diva-23086Test
Current opinion in chemical biology, 1367-5931, 2006, 10:5, s. 473-479
الإتاحة: Open access content. Open access content
info:eu-repo/semantics/restrictedAccess
ملاحظة: English
أرقام أخرى: UPE oai:DiVA.org:uu-23086
doi:doi:10.1016/j.cbpa.2006.08.015
PMID 16938485
1235071340
المصدر المساهم: UPPSALA UNIV LIBR
From OAIster®, provided by the OCLC Cooperative.
رقم الانضمام: edsoai.on1235071340
قاعدة البيانات: OAIster