Structure and function of allophanate hydrolase

Chen Fan; Zi Li; Huiyong Yin; Song Xiang

doi:10.1074/jbc.M113.453837

Structure and function of allophanate hydrolase

Research output: Journal Publications and Reviews › RGC 21 - Publication in refereed journal › peer-review

Overview

21 Scopus Citations

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Author(s)

Chen Fan
Zi Li
Huiyong Yin
Song Xiang

Detail(s)

Original language	English
Pages (from-to)	21422-21432
Journal / Publication	Journal of Biological Chemistry
Volume	288
Issue number	29
Publication status	Published - 19 Jul 2013
Externally published	Yes

Link(s)

DOI	DOI https://doi.org/10.1074/jbc.M113.453837 Final Published version
	Check@CityULib
Attachment(s)	Documents 143104934.pdf Final Published version, 3.46 MB, PDF Publisher's Copyright Statement This full text is made available under CC-BY 4.0. https://creativecommons.org/licenses/by/4.0/
Link to Scopus	https://www.scopus.com/record/display.uri?eid=2-s2.0-84880518748&origin=recordpage
Permanent Link	https://scholars.cityu.edu.hk/en/publications/publication(cfb5bd7f-c1b4-460d-9039-2cf60db3c5d2).html

Abstract

Background: Allophanate hydrolase (AH) is essential for urea utilization in many organisms. Results: We determined the crystal structure of the Kluyveromyces lactis AH and performed mechanistic studies. Conclusion: Our work revealed that the AH N and C domains catalyze sequential reactions and provided insights into their catalysis. Significance: The catalytic mechanism of the C domain might expand the knowledge of decarboxylation reactions. © 2013 by The American Society for Biochemistry and Molecular Biology, Inc.

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