Multienzyme complexes

Multienzyme complexes are stable assemblies of more than one enzyme, generally involved in sequential catalytic transformations. These are distinct from a multienzyme polypeptide, in which multiple catalytic domains are found in a single polypeptide chain. Fatty-acyl-CoA Synthase is an example of six enzymes that assemble in a barrel shape to generate fatty acids.

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  • Research |

    The function of putative bacterial vitamin K-dependent carboxylases (VKDCs) has so far been uncertain. Now, Micklefield and co-workers show that a bacterial VKDC orthologue is involved in the biosynthesis of the antibiotic malonomycin, generating an unusual malonic acid moiety that is essential for its biological activity.

    • Brian J. C. Law
    • , Ying Zhuo
    • , Michael Winn
    • , Daniel Francis
    • , Yingxin Zhang
    • , Markiyan Samborskyy
    • , Annabel Murphy
    • , Lujing Ren
    • , Peter F. Leadlay
    •  & Jason Micklefield
    Nature Catalysis 1, 977-984
  • Research | | open

    Mitochondrial protein synthesis requires charging a mitochondrial tRNA with its amino acid. Here, the authors describe pathogenic variants in the GatCAB protein complex genes required for the generation of glutaminyl-mt-tRNAGln, that impairs mitochondrial translation and presents with cardiomyopathy.

    • Marisa W. Friederich
    • , Sharita Timal
    • , Christopher A. Powell
    • , Cristina Dallabona
    • , Alina Kurolap
    • , Sara Palacios-Zambrano
    • , Drago Bratkovic
    • , Terry G. J. Derks
    • , David Bick
    • , Katelijne Bouman
    • , Kathryn C. Chatfield
    • , Nadine Damouny-Naoum
    • , Megan K. Dishop
    • , Tzipora C. Falik-Zaccai
    • , Fuad Fares
    • , Ayalla Fedida
    • , Ileana Ferrero
    • , Renata C. Gallagher
    • , Rafael Garesse
    • , Micol Gilberti
    • , Cristina González
    • , Katherine Gowan
    • , Clair Habib
    • , Rebecca K. Halligan
    • , Limor Kalfon
    • , Kaz Knight
    • , Dirk Lefeber
    • , Laura Mamblona
    • , Hanna Mandel
    • , Adi Mory
    • , John Ottoson
    • , Tamar Paperna
    • , Ger J. M. Pruijn
    • , Pedro F. Rebelo-Guiomar
    • , Ann Saada
    • , Bruno Sainz Jr.
    • , Hayley Salvemini
    • , Mirthe H. Schoots
    • , Jan A. Smeitink
    • , Maciej J. Szukszto
    • , Hendrik J. ter Horst
    • , Frans van den Brandt
    • , Francjan J. van Spronsen
    • , Joris A. Veltman
    • , Eric Wartchow
    • , Liesbeth T. Wintjes
    • , Yaniv Zohar
    • , Miguel A. Fernández-Moreno
    • , Hagit N. Baris
    • , Claudia Donnini
    • , Michal Minczuk
    • , Richard J. Rodenburg
    •  & Johan L. K. Van Hove
  • Research | | open

    Modifying the non-ribosomal peptide synthase (NRPS)/polyketide synthase (PKS) pathway to generate novel non-ribosomal peptides often results in a loss of productivity. Here the authors use evolutionary alignments of NRPS/PKS gene clusters to guide rational design of complexes that can produce novel lactones.

    • Takayoshi Awakawa
    • , Takuma Fujioka
    • , Lihan Zhang
    • , Shotaro Hoshino
    • , Zhijuan Hu
    • , Junko Hashimoto
    • , Ikuko Kozone
    • , Haruo Ikeda
    • , Kazuo Shin-Ya
    • , Wen Liu
    •  & Ikuro Abe
  • Research | | open

    Catabolizing lignin-derived aromatic compounds requires an aryl-O-demethylation step. Here the authors present the structures of GcoA and GcoB, a cytochrome P450-reductase pair that catalyzes aryl-O-demethylations and show that GcoA displays broad substrate specificity, which is of interest for biotechnology applications.

    • Sam J. B. Mallinson
    • , Melodie M. Machovina
    • , Rodrigo L. Silveira
    • , Marc Garcia-Borràs
    • , Nathan Gallup
    • , Christopher W. Johnson
    • , Mark D. Allen
    • , Munir S. Skaf
    • , Michael F. Crowley
    • , Ellen L. Neidle
    • , Kendall N. Houk
    • , Gregg T. Beckham
    • , Jennifer L. DuBois
    •  & John E. McGeehan

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