رسالة جامعية
Substrate Channeling via a Transient Protein-Protein Complex: : The case of D-Glyceraldehyde-3-Phosphate Dehydrogenase and L-Lactate Dehydrogenase. ; Provođenje supstrata preko prijelaznog protein-protein kompleksa: : Slučaj D-gliceraldehid-3-fosfat dehidrogenaze i L-laktat dehidrogenaze
| العنوان: | Substrate Channeling via a Transient Protein-Protein Complex: : The case of D-Glyceraldehyde-3-Phosphate Dehydrogenase and L-Lactate Dehydrogenase. ; Provođenje supstrata preko prijelaznog protein-protein kompleksa: : Slučaj D-gliceraldehid-3-fosfat dehidrogenaze i L-laktat dehidrogenaze |
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| المؤلفون: | Martinović, Manuel |
| المساهمون: | Svedružić, Željko |
| بيانات النشر: | Sveučilište u Rijeci. Odjel za biotehnologiju. University of Rijeka. Department of Biotechnology. |
| سنة النشر: | 2019 |
| المجموعة: | Repository of the University of Rijeka |
| مصطلحات موضوعية: | D-Glyceraldehyde-3-Phosphate Dehydrogenase, L-Lactate Dehydrogenase, D-gliceraldehid-3-fosfat dehidrogenaze, L-laktat dehidrogenaze, BIOTEHNIČKE ZNANOSTI. Biotehnologija, BIOTECHNICAL SCIENCES. Biotechnology |
| الوصف: | NADH channeling from D-Glyceraldehyde-3-phosphate dehydrogenase (GAPDH) to L-Lactate dehydrogenase (LDH) can regulate the major metabolic pathways. We have investigated possible NADH channeling from GAPDH to LDH isozymes using enzymes from different cells Numerous non-computational experimental data has shown that NADH is channeled through GAPDH to LDH through a transient protein complex: analytical ultracentrifugation and enzyme-kinetics studies showed that GAPDH molecules can channel their NADH substrate to LDH molecules via a transient LDH-GAPDH complex. Michaelis–Menten constants for LDH activity in channeling and diffusive reactions depend on the extent of GAPDH saturation with NADH substrate. Different molecular dynamics approaches (all-atom and coarse-grained models) showed that LDH and GAPDH tetramers can form a complex that breaks down when the enzymes are saturated with NADH molecules. LDH and GAPDH tetramers form a complex that can simultaneously support channeled and diffusive reactions as a part of a large supramolecular complex. The interaction sites are conserved between LDH isozymes from heart and muscle, and between GAPDH molecules from rabbit and yeast cells. Positive electric fields between the NAD(H) binding sites in LDH and GAPDH tetramers showed that NAD(H)-channeling within the LDH-GAPDH complex can be an extension of NAD(H)-channeling between the adjacent subunits in each tetramer. ; Provođenje NADH substrata od D-gliceraldehid-3-fosfat dehidrogenaze (GAPDH) do L-laktat-dehidrogenaze (LDH) može regulirati glavne metaboličke puteve. Istražili smo mogući naćin prosljiđivanja NADH kroz ova dva enzima, koristeći I enzime iz raznih organizama. Brojni ne-računalni podaci upućuju na prosljeđivanje NADH kroz tranzicijski protein kompleks LDH i GAPDH. Studije analitičke ultracentrifugacije i enzimske kinetike upućuju na mogucnost proslijediivanja NADH od GAPDH do LDH preko takvog kompleksa, a Michaelis-Menten konsante za aktivnost LDH u reakcijama vodjenim difucijom I reakcijama vodjenim ... |
| نوع الوثيقة: | bachelor thesis |
| وصف الملف: | application/pdf |
| اللغة: | English |
| العلاقة: | https://www.unirepository.svkri.uniri.hr/islandora/object/biotechri:420Test; https://urn.nsk.hr/urn:nbn:hr:193:559771Test; https://www.unirepository.svkri.uniri.hr/islandora/object/biotechri:420/datastream/PDFTest |
| الإتاحة: | https://www.unirepository.svkri.uniri.hr/islandora/object/biotechri:420Test https://urn.nsk.hr/urn:nbn:hr:193:559771Test https://www.unirepository.svkri.uniri.hr/islandora/object/biotechri:420/datastream/PDFTest |
| حقوق: | http://rightsstatements.org/vocab/InC/1.0Test/ ; info:eu-repo/semantics/restrictedAccess |
| رقم الانضمام: | edsbas.B6126D43 |
| قاعدة البيانات: | BASE |
| الوصف غير متاح. |