Bacterial expression of human kynurenine 3-monooxygenase: Solubility, activity, purification☆

•This is the first report of soluble and active bacterially expressed human KMO protein.•Partial purification of the enzyme was achieved and the two protein co-elutants identified.•Steady state kinetic parameters were comparable to those reported for mammalian expressed.•The C-terminal membrane targ...

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Main Authors:	Wilson, K., Mole, D.J., Binnie, M., Homer, N.Z.M., Zheng, X., Yard, B.A., Iredale, J.P., Auer, M., Webster, S.P.
Format:	Online
Language:	English
Published:	Academic Press 2014
Online Access:	https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3969302/

id	pubmed-3969302
recordtype	oai_dc
spelling	pubmed-39693022014-03-31 Bacterial expression of human kynurenine 3-monooxygenase: Solubility, activity, purification☆ Wilson, K. Mole, D.J. Binnie, M. Homer, N.Z.M. Zheng, X. Yard, B.A. Iredale, J.P. Auer, M. Webster, S.P. Article •This is the first report of soluble and active bacterially expressed human KMO protein.•Partial purification of the enzyme was achieved and the two protein co-elutants identified.•Steady state kinetic parameters were comparable to those reported for mammalian expressed.•The C-terminal membrane targetting domain of human KMO is required for its enzymatic activity. Academic Press 2014-03 /pmc/articles/PMC3969302/ /pubmed/24316190 http://dx.doi.org/10.1016/j.pep.2013.11.015 Text en © 2013 The Authors http://creativecommons.org/licenses/by/3.0/ This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited.
repository_type	Open Access Journal
institution_category	Foreign Institution
institution	US National Center for Biotechnology Information
building	NCBI PubMed
collection	Online Access
language	English
format	Online
author	Wilson, K. Mole, D.J. Binnie, M. Homer, N.Z.M. Zheng, X. Yard, B.A. Iredale, J.P. Auer, M. Webster, S.P.
spellingShingle	Wilson, K. Mole, D.J. Binnie, M. Homer, N.Z.M. Zheng, X. Yard, B.A. Iredale, J.P. Auer, M. Webster, S.P. Bacterial expression of human kynurenine 3-monooxygenase: Solubility, activity, purification☆
author_facet	Wilson, K. Mole, D.J. Binnie, M. Homer, N.Z.M. Zheng, X. Yard, B.A. Iredale, J.P. Auer, M. Webster, S.P.
author_sort	Wilson, K.
title	Bacterial expression of human kynurenine 3-monooxygenase: Solubility, activity, purification☆
title_short	Bacterial expression of human kynurenine 3-monooxygenase: Solubility, activity, purification☆
title_full	Bacterial expression of human kynurenine 3-monooxygenase: Solubility, activity, purification☆
title_fullStr	Bacterial expression of human kynurenine 3-monooxygenase: Solubility, activity, purification☆
title_full_unstemmed	Bacterial expression of human kynurenine 3-monooxygenase: Solubility, activity, purification☆
title_sort	bacterial expression of human kynurenine 3-monooxygenase: solubility, activity, purification☆
description	•This is the first report of soluble and active bacterially expressed human KMO protein.•Partial purification of the enzyme was achieved and the two protein co-elutants identified.•Steady state kinetic parameters were comparable to those reported for mammalian expressed.•The C-terminal membrane targetting domain of human KMO is required for its enzymatic activity.
publisher	Academic Press
publishDate	2014
url	https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3969302/
_version_	1612072294087131136

Bacterial expression of human kynurenine 3-monooxygenase: Solubility, activity, purification☆

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