Cargando…

Mutations of an NAD(P)H-dependent flavoprotein monooxygenase that influence cofactor promiscuity and enantioselectivity()

The flavoprotein monooxygenase (FPMO) from Stenotrophomonas maltophilia (SMFMO, Uniprot: B2FLR2) catalyses the asymmetric oxidation of thioethers and is unusual amongst FPMOs in its ability to use the non-phosphorylated cofactor NADH, as well as NADPH, for the reduction of the FAD coenzyme. In order...

Descripción completa

Detalles Bibliográficos
Autores principales:	Jensen, Chantel N., Ali, Sohail T., Allen, Michael J., Grogan, Gideon
Formato:	Online Artículo Texto
Lenguaje:	English
Publicado:	Elsevier 2013
Materias:	Article
Acceso en línea:	https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3829993/ https://www.ncbi.nlm.nih.gov/pubmed/24251114 http://dx.doi.org/10.1016/j.fob.2013.09.008

Ejemplares similares

Exploring nicotinamide cofactor promiscuity in NAD(P)H-dependent flavin containing monooxygenases (FMOs) using natural variation within the phosphate binding loop. Structure and activity of FMOs from Cellvibrio sp. BR and Pseudomonas stutzeri NF13
por: Jensen, Chantel N., et al.
Publicado: (2014)

Functional and structural characterization of a flavoprotein monooxygenase essential for biogenesis of tryptophylquinone cofactor
por: Oozeki, Toshinori, et al.
Publicado: (2021)

Developing and enhancing promiscuous activity for NAD(P)H-dependent flavin reductase via elimination of cofactor
por: Navaser, Amene, et al.
Publicado: (2023)

Flavoprotein monooxygenases for oxidative biocatalysis: recombinant expression in microbial hosts and applications
por: Ceccoli, Romina D., et al.
Publicado: (2014)

The Phylogeny of Class B Flavoprotein Monooxygenases and the Origin of the YUCCA Protein Family
por: Turnaev, Igor I., et al.
Publicado: (2020)

Remaining challenges in cellular flavin cofactor homeostasis and flavoprotein biogenesis
por: Giancaspero, Teresa A., et al.
Publicado: (2015)

Form Follows Function: Structural and Catalytic Variation in the Class A Flavoprotein Monooxygenases
por: Crozier-Reabe, Karen, et al.
Publicado: (2012)

Pyridine Nucleotide Coenzyme Specificity of p-Hydroxybenzoate Hydroxylase and Related Flavoprotein Monooxygenases
por: Westphal, Adrie H., et al.
Publicado: (2018)

The 2′-hydroxy group of flavin mononucleotide influences the catalytic function and promiscuity of the flavoprotein iodotyrosine dehalogenase
por: Kozyryev, Anton, et al.
Publicado: (2023)

Oxidation of the FAD cofactor to the 8-formyl-derivative in human electron-transferring flavoprotein
por: Augustin, Peter, et al.
Publicado: (2018)

Using Intrinsic Flavoprotein and NAD(P)H Imaging to Map Functional Circuitry in the Main Olfactory Bulb
por: Uytingco, Cedric R., et al.
Publicado: (2016)

The Iron-Sulfur Flavoprotein DsrL as NAD(P)H:Acceptor Oxidoreductase in Oxidative and Reductive Dissimilatory Sulfur Metabolism
por: Löffler, Maria, et al.
Publicado: (2020)

Mutations Increasing Cofactor Affinity, Improve Stability and Activity of a Baeyer–Villiger Monooxygenase
por: Mansouri, Hamid R., et al.
Publicado: (2022)

Biocatalytic Conversion of Cyclic Ketones Bearing α‐Quaternary Stereocenters into Lactones in an Enantioselective Radical Approach to Medium‐Sized Carbocycles
por: Morrill, Charlotte, et al.
Publicado: (2018)

NAD(P)H‐Dependent Dehydrogenases for the Asymmetric Reductive Amination of Ketones: Structure, Mechanism, Evolution and Application
por: Sharma, Mahima, et al.
Publicado: (2017)

Erratum: The Iron-Sulfur Flavoprotein DsrL as NAD(P)H:Acceptor Oxidoreductase in Oxidative and Reductive Dissimilatory Sulfur Metabolism
por: Frontiers Production Office,
Publicado: (2021)

Structures of the Apo and FAD-Bound Forms of 2-Hydroxybiphenyl 3-monooxygenase (HbpA) Locate Activity Hotspots Identified by Using Directed Evolution
por: Jensen, Chantel N, et al.
Publicado: (2015)

Evidence that the nadA motif is a bacterial riboswitch for the ubiquitous enzyme cofactor NAD(+)
por: Malkowski, Sarah N., et al.
Publicado: (2019)

Modular Assembly of Phosphite Dehydrogenase and Phenylacetone Monooxygenase for Tuning Cofactor Regeneration
por: Purwani, Ni Nyoman, et al.
Publicado: (2021)

A second riboswitch class for the enzyme cofactor NAD(+)
por: Panchapakesan, Shanker S.S., et al.
Publicado: (2021)

Plant Flavoprotein Photoreceptors
por: Christie, John M., et al.
Publicado: (2015)

Spin Dynamics of Flavoproteins
por: Matysik, Jörg, et al.
Publicado: (2023)

Mycofactocin-associated mycobacterial dehydrogenases with non-exchangeable NAD cofactors
por: Haft, Daniel H., et al.
Publicado: (2017)

A Versatile Chemoenzymatic Nanoreactor that Mimics NAD(P)H Oxidase for the In Situ Regeneration of Cofactors
por: Rodriguez‐Abetxuko, Andoni, et al.
Publicado: (2022)

Network-wide thermodynamic constraints shape NAD(P)H cofactor specificity of biochemical reactions
por: Bekiaris, Pavlos Stephanos, et al.
Publicado: (2023)

Vertebrate Cryptochromes are Vestigial Flavoproteins
por: Kutta, Roger J., et al.
Publicado: (2017)

Using mutability landscapes of a promiscuous tautomerase to guide the engineering of enantioselective Michaelases
por: van der Meer, Jan-Ytzen, et al.
Publicado: (2016)

Cofactor engineering to regulate NAD(+)/NADH ratio with its application to phytosterols biotransformation
por: Su, Liqiu, et al.
Publicado: (2017)

Ferroptosis-Related Flavoproteins: Their Function and Stability
por: Vabulas, R. Martin
Publicado: (2021)

A Phosphite Dehydrogenase Variant with Promiscuous Access to Nicotinamide Cofactor Pools Sustains Fast Phosphite-Dependent Growth of Transplastomic Chlamydomonas reinhardtii
por: Cutolo, Edoardo, et al.
Publicado: (2020)

Catalytic and hydrodynamic properties of styrene monooxygenases from Rhodococcus opacus 1CP are modulated by cofactor binding
por: Riedel, Anika, et al.
Publicado: (2015)

Peculiarities of promiscuous l-threonine transaldolases for enantioselective synthesis of β-hydroxy-α-amino acids
por: Wang, Shan, et al.
Publicado: (2021)

A Regulatory Role of NAD Redox Status on Flavin Cofactor Homeostasis in S. cerevisiae Mitochondria
por: Giancaspero, Teresa Anna, et al.
Publicado: (2013)

Structural Basis of Redox-Sensing Transcriptional Repressor Rex with Cofactor NAD(+) and Operator DNA
por: Jeong, Kang Hwa, et al.
Publicado: (2022)

EGFRvIII: the promiscuous mutation
por: Greenall, Sameer A, et al.
Publicado: (2016)

Mechanisms of Reaction of Some Flavoprotein Enzymes with Oxygen
por: Gibson, Quentin H.
Publicado: (1965)

Catalases Are NAD(P)H-Dependent Tellurite Reductases
por: Calderón, Iván L., et al.
Publicado: (2006)

Mutations make gut antibodies promiscuous
por: Grasset, Emilie K., et al.
Publicado: (2020)

Evolution of Function in the “Two Dinucleotide Binding Domains” Flavoproteins
por: Ojha, Sunil, et al.
Publicado: (2007)

Long-Time Oxygen Localization in Electron Transfer Flavoprotein
por: Salerno, K. Michael, et al.
Publicado: (2022)

Cannot write session to /tmp/vufind_sessions/sess_lb9706f0ds7squd72ulcl57heb