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undergraduate thesis
Substrate Channeling via a Transient Protein-Protein Complex:
The case of D-Glyceraldehyde-3-Phosphate Dehydrogenase and L-Lactate Dehydrogenase.
2019. urn:nbn:hr:193:559771
Martinović, Manuel
University of Rijeka
Faculty of Biotechnology and Drug Development

Cite this document

Martinović, M. (2019). Substrate Channeling via a Transient Protein-Protein Complex: : The case of D-Glyceraldehyde-3-Phosphate Dehydrogenase and L-Lactate Dehydrogenase. (Undergraduate thesis). Rijeka: University of Rijeka. Retrieved from https://urn.nsk.hr/urn:nbn:hr:193:559771

Martinović, Manuel. "Substrate Channeling via a Transient Protein-Protein Complex: : The case of D-Glyceraldehyde-3-Phosphate Dehydrogenase and L-Lactate Dehydrogenase.." Undergraduate thesis, University of Rijeka, 2019. https://urn.nsk.hr/urn:nbn:hr:193:559771

Martinović, Manuel. "Substrate Channeling via a Transient Protein-Protein Complex: : The case of D-Glyceraldehyde-3-Phosphate Dehydrogenase and L-Lactate Dehydrogenase.." Undergraduate thesis, University of Rijeka, 2019. https://urn.nsk.hr/urn:nbn:hr:193:559771

Martinović, M. (2019). 'Substrate Channeling via a Transient Protein-Protein Complex: : The case of D-Glyceraldehyde-3-Phosphate Dehydrogenase and L-Lactate Dehydrogenase.', Undergraduate thesis, University of Rijeka, accessed 17 November 2024, https://urn.nsk.hr/urn:nbn:hr:193:559771

Martinović M. Substrate Channeling via a Transient Protein-Protein Complex: : The case of D-Glyceraldehyde-3-Phosphate Dehydrogenase and L-Lactate Dehydrogenase. [Undergraduate thesis]. Rijeka: University of Rijeka; 2019 [cited 2024 November 17] Available at: https://urn.nsk.hr/urn:nbn:hr:193:559771

M. Martinović, "Substrate Channeling via a Transient Protein-Protein Complex: : The case of D-Glyceraldehyde-3-Phosphate Dehydrogenase and L-Lactate Dehydrogenase.", Undergraduate thesis, University of Rijeka, Rijeka, 2019. Available at: https://urn.nsk.hr/urn:nbn:hr:193:559771

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Metadata
TitleSubstrate Channeling via a Transient Protein-Protein Complex: : The case of D-Glyceraldehyde-3-Phosphate Dehydrogenase and L-Lactate Dehydrogenase.
Title (croatian)Provođenje supstrata preko prijelaznog protein-protein kompleksa: : Slučaj D-gliceraldehid-3-fosfat dehidrogenaze i L-laktat dehidrogenaze
AuthorManuel Martinović
MentorŽeljko Svedružić (mentor)
Committee memberJasminka Giacometti (predsjednik povjerenstva)
Committee memberKarlo Wittine (član povjerenstva)
Committee memberŽeljko Svedružić (član povjerenstva)
GranterUniversity of Rijeka
(Faculty of Biotechnology and Drug Development)
Rijeka
Defense date and country2019, Croatia
Scientific / art field,
discipline and subdiscipline		BIOTECHNICAL SCIENCES
Biotechnology
Abstract
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.
Abstract (croatian)
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 proslijedjivanjem substrata, pokazuju ovisnost o zasicenosti GAPDH sa NADH substratom. Različite tehnike računalne molekularne dinamike (all-atom i coarse-grained modeli molekularne dinamike) prikazuju kompleks ova dva enzima koji se raspada zasićenjem sa NADH. LDH i GAPDH mogu provoditi reakcije vođene difuzijom i vođene proslijeđivanjem substrata kao dio višemolekulskog kompleksa. Interaktivna mjesta su očuvana izmedju izoenzima LDH iz srca i mišića sisavaca, te GAPDH iz sisavca (zec) i pekarskog kvasca. Pozitivni električni naboj izmedju NADH vezujućih mjesta ova tetramera LDH i GAPDH pokazuju kako proslijeđivanje NADH moze biti proširenje modela koji govori o proslijeđivanju istog substarta medju susjednim podjedinicama svakog tetramera.
Keywords
Keywords (croatian)
Languageenglish
URN:NBNurn:nbn:hr:193:559771
Study programmeTitle: Biotechnology and drug research
Study programme type: university
Study level: undergraduate
Academic / professional title: sveučilišni/a prvostupnik/prvostupnica biotehnologije i istraživanja lijekova (sveučilišni/a prvostupnik/prvostupnica biotehnologije i istraživanja lijekova)
Type of resourceText
File originBorn digital
Access conditionsAccess restricted to students and staff of home institution
Terms of useLicence In copyright icon
Created on2019-11-04 09:17:17