000134624 001__ 134624
000134624 005__ 20260217205502.0
000134624 0247_ $$2doi$$a10.1002/pro.4984
000134624 0248_ $$2sideral$$a138317
000134624 037__ $$aART-2024-138317
000134624 041__ $$aeng
000134624 100__ $$aLedesma-Fernandez, Alba
000134624 245__ $$aEngineering bio-brick protein scaffolds for organizing enzyme assemblies
000134624 260__ $$c2024
000134624 5203_ $$aEnzyme scaffolding is an emerging approach for enhancing the catalytic efficiency of multi‐enzymatic cascades by controlling their spatial organization and stoichiometry. This study introduces a novel family of engineered SCAffolding Bricks, named SCABs, utilizing the consensus tetratricopeptide repeat (CTPR) domain for organized multi‐enzyme systems. Two SCAB systems are developed, one employing head‐to‐tail interactions with reversible covalent disulfide bonds, the other relying on non‐covalent metal‐driven assembly via engineered metal coordinating interfaces. Enzymes are directly fused to SCAB modules, triggering assembly in a non‐reducing environment or by metal presence. A proof‐of‐concept with formate dehydrogenase (FDH) and L‐alanine dehydrogenase (AlaDH) shows enhanced specific productivity by 3.6‐fold compared to free enzymes, with the covalent stapling outperforming the metal‐driven assembly. This enhancement likely stems from higher‐order supramolecular assembly and improved NADH cofactor regeneration, resulting in more efficient cascades. This study underscores the potential of protein engineering to tailor scaffolds, leveraging supramolecular spatial‐organizing tools, for more efficient enzymatic cascade reactions.
000134624 536__ $$9info:eu-repo/grantAgreement/ES/AEI/PID2019-111649RB-I00$$9info:eu-repo/grantAgreement/EC/Era-CoBiotech/HOMBIOCAT/PCI2018-092984$$9info:eu-repo/grantAgreement/ES/MICINN AEI/PID2022-137977OB-I00
000134624 540__ $$9info:eu-repo/semantics/openAccess$$aAll rights reserved$$uhttp://www.europeana.eu/rights/rr-f/
000134624 590__ $$a5.2$$b2024
000134624 592__ $$a4.657$$b2024
000134624 591__ $$aBIOCHEMISTRY & MOLECULAR BIOLOGY$$b68 / 320 = 0.213$$c2024$$dQ1$$eT1
000134624 593__ $$aBiochemistry$$c2024$$dQ1
000134624 593__ $$aMolecular Biology$$c2024$$dQ1
000134624 593__ $$aMedicine (miscellaneous)$$c2024$$dQ1
000134624 594__ $$a12.4$$b2024
000134624 655_4 $$ainfo:eu-repo/semantics/article$$vinfo:eu-repo/semantics/publishedVersion
000134624 700__ $$aVelasco-Lozano, Susana
000134624 700__ $$aCampos-Muelas, Pedro
000134624 700__ $$aMadrid, Ricardo
000134624 700__ $$0(orcid)0000-0003-0031-1880$$aLópez-Gallego, Fernando
000134624 700__ $$aCortajarena, Aitziber L.
000134624 773__ $$g33, 5 (2024), e4984 [17 pp.]$$pProtein sci.$$tProtein science$$x0961-8368
000134624 8564_ $$s13930602$$uhttps://zaguan.unizar.es/record/134624/files/texto_completo.pdf$$yVersión publicada
000134624 8564_ $$s2046752$$uhttps://zaguan.unizar.es/record/134624/files/texto_completo.jpg?subformat=icon$$xicon$$yVersión publicada
000134624 909CO $$ooai:zaguan.unizar.es:134624$$particulos$$pdriver
000134624 951__ $$a2026-02-17-20:22:28
000134624 980__ $$aARTICLE