Literature DB >> 18280246

The growing VAO flavoprotein family.

Nicole G H Leferink1, Dominic P H M Heuts, Marco W Fraaije, Willem J H van Berkel.   

Abstract

The VAO flavoprotein family is a rapidly growing family of oxidoreductases that favor the covalent binding of the FAD cofactor. In this review we report on the catalytic properties of some newly discovered VAO family members and their mode of flavin binding. Covalent binding of the flavin is a self-catalytic post-translational modification primarily taking place in oxidases. Covalent flavinylation increases the redox potential of the cofactor and thus its oxidation power. Recent findings have revealed that some members of the VAO family anchor the flavin via a dual covalent linkage (6-S-cysteinyl-8alpha-N1-histidyl FAD). Some VAO-type aldonolactone oxidoreductases favor the non-covalent binding of the flavin cofactor. These enzymes act as dehydrogenases, using cytochrome c as electron acceptor.

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Year:  2008        PMID: 18280246     DOI: 10.1016/j.abb.2008.01.027

Source DB:  PubMed          Journal:  Arch Biochem Biophys        ISSN: 0003-9861            Impact factor:   4.013


  31 in total

Review 1.  Recent progress on the characterization of aldonolactone oxidoreductases.

Authors:  Siddique I Aboobucker; Argelia Lorence
Journal:  Plant Physiol Biochem       Date:  2015-11-27       Impact factor: 4.270

2.  Two tyrosine residues, Tyr-108 and Tyr-503, are responsible for the deprotonation of phenolic substrates in vanillyl-alcohol oxidase.

Authors:  Tom A Ewing; Quoc-Thai Nguyen; Robert C Allan; Gudrun Gygli; Elvira Romero; Claudia Binda; Marco W Fraaije; Andrea Mattevi; Willem J H van Berkel
Journal:  J Biol Chem       Date:  2017-07-17       Impact factor: 5.157

3.  Evolutionary history of D-lactate dehydrogenases: a phylogenomic perspective on functional diversity in the FAD binding oxidoreductase/transferase type 4 family.

Authors:  Melania E Cristescu; Emmanuel E Egbosimba
Journal:  J Mol Evol       Date:  2009-09       Impact factor: 2.395

4.  The crystal structure and mechanism of an unusual oxidoreductase, GilR, involved in gilvocarcin V biosynthesis.

Authors:  Nicholas Noinaj; Mary A Bosserman; M Alexandra Schickli; Grzegorz Piszczek; Madan K Kharel; Pallab Pahari; Susan K Buchanan; Jürgen Rohr
Journal:  J Biol Chem       Date:  2011-05-10       Impact factor: 5.157

5.  Structural basis of inhibition of Mycobacterium tuberculosis DprE1 by benzothiazinone inhibitors.

Authors:  Sarah M Batt; Talat Jabeen; Veemal Bhowruth; Lee Quill; Peter A Lund; Lothar Eggeling; Luke J Alderwick; Klaus Fütterer; Gurdyal S Besra
Journal:  Proc Natl Acad Sci U S A       Date:  2012-06-25       Impact factor: 11.205

6.  Vacuole-localized berberine bridge enzyme-like proteins are required for a late step of nicotine biosynthesis in tobacco.

Authors:  Masataka Kajikawa; Tsubasa Shoji; Akira Kato; Takashi Hashimoto
Journal:  Plant Physiol       Date:  2011-02-22       Impact factor: 8.340

7.  Discovery of a Xylooligosaccharide Oxidase from Myceliophthora thermophila C1.

Authors:  Alessandro R Ferrari; Henriëtte J Rozeboom; Justyna M Dobruchowska; Sander S van Leeuwen; Aniek S C Vugts; Martijn J Koetsier; Jaap Visser; Marco W Fraaije
Journal:  J Biol Chem       Date:  2016-09-14       Impact factor: 5.157

8.  Functional roles of the 6-S-cysteinyl, 8alpha-N1-histidyl FAD in glucooligosaccharide oxidase from Acremonium strictum.

Authors:  Chun-Hsiang Huang; Andreas Winkler; Chia-Lin Chen; Wen-Lin Lai; Ying-Chieh Tsai; Peter Macheroux; Shwu-Huey Liaw
Journal:  J Biol Chem       Date:  2008-09-03       Impact factor: 5.157

9.  Structural and mechanistic studies reveal the functional role of bicovalent flavinylation in berberine bridge enzyme.

Authors:  Andreas Winkler; Kerstin Motz; Sabrina Riedl; Martin Puhl; Peter Macheroux; Karl Gruber
Journal:  J Biol Chem       Date:  2009-05-19       Impact factor: 5.157

Review 10.  Oxidation of amines by flavoproteins.

Authors:  Paul F Fitzpatrick
Journal:  Arch Biochem Biophys       Date:  2009-08-03       Impact factor: 4.013

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