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Structure-Based Mechanism for Early PLP-Mediated Steps of Rabbit Cytosolic Serine Hydroxymethyltransferase Reaction
المؤلفون المشاركون
di Salvo, Martino Luigi
Scarsdale, J. Neel
Kazanina, Galina
Schirch, Verne
Wright, H. Tonie
Contestabile, Roberto
المصدر
العدد
المجلد 2013، العدد 2013 (31 ديسمبر/كانون الأول 2013)، ص ص. 1-13، 13ص.
الناشر
Hindawi Publishing Corporation
تاريخ النشر
2013-07-15
دولة النشر
مصر
عدد الصفحات
13
التخصصات الرئيسية
الملخص EN
Serine hydroxymethyltransferase catalyzes the reversible interconversion of L-serine and glycine with transfer of one-carbon groups to and from tetrahydrofolate.
Active site residue Thr254 is known to be involved in the transaldimination reaction, a crucial step in the catalytic mechanism of all pyridoxal 5′-phosphate- (PLP-) dependent enzymes, which determines binding of substrates and release of products.
In order to better understand the role of Thr254, we have expressed, characterized, and determined the crystal structures of rabbit cytosolic serine hydroxymethyltransferase T254A and T254C mutant forms, in the absence and presence of substrates.
These mutants accumulate a kinetically stable gem-diamine intermediate, and their crystal structures show differences in the active site with respect to wild type.
The kinetic and crystallographic data acquired with mutant enzymes permit us to infer that conversion of gem-diamine to external aldimine is significantly slowed because intermediates are trapped into an anomalous position by a misorientation of the PLP ring, and a new energy barrier hampers the transaldimination reaction.
This barrier likely arises from the loss of the stabilizing hydrogen bond between the hydroxymethyl group of Thr254 and the ε-amino group of active site Lys257, which stabilizes the external aldimine intermediate in wild type SHMTs.
نمط استشهاد جمعية علماء النفس الأمريكية (APA)
di Salvo, Martino Luigi& Scarsdale, J. Neel& Kazanina, Galina& Contestabile, Roberto& Schirch, Verne& Wright, H. Tonie. 2013. Structure-Based Mechanism for Early PLP-Mediated Steps of Rabbit Cytosolic Serine Hydroxymethyltransferase Reaction. BioMed Research International،Vol. 2013, no. 2013, pp.1-13.
https://search.emarefa.net/detail/BIM-1030557
نمط استشهاد الجمعية الأمريكية للغات الحديثة (MLA)
di Salvo, Martino Luigi…[et al.]. Structure-Based Mechanism for Early PLP-Mediated Steps of Rabbit Cytosolic Serine Hydroxymethyltransferase Reaction. BioMed Research International No. 2013 (2013), pp.1-13.
https://search.emarefa.net/detail/BIM-1030557
نمط استشهاد الجمعية الطبية الأمريكية (AMA)
di Salvo, Martino Luigi& Scarsdale, J. Neel& Kazanina, Galina& Contestabile, Roberto& Schirch, Verne& Wright, H. Tonie. Structure-Based Mechanism for Early PLP-Mediated Steps of Rabbit Cytosolic Serine Hydroxymethyltransferase Reaction. BioMed Research International. 2013. Vol. 2013, no. 2013, pp.1-13.
https://search.emarefa.net/detail/BIM-1030557
نوع البيانات
مقالات
لغة النص
الإنجليزية
الملاحظات
Includes bibliographical references
رقم السجل
BIM-1030557
قاعدة معامل التأثير والاستشهادات المرجعية العربي "ارسيف Arcif"
أضخم قاعدة بيانات عربية للاستشهادات المرجعية للمجلات العلمية المحكمة الصادرة في العالم العربي
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