Expression, Purification, Crystallization And Preliminary X-Ray Studies of Histamine Dehydrogenase From Nocardioides Simplex
Abstract
Histamine dehydrogenase (HADH) from Nocardioides simplex catalyzes the oxidative deamination of histamine to produce imidazole acetaldehyde and an ammonium ion. HADH is functionally related to trimethylamine dehydrogenase (TMADH), but HADH has strict substrate specificity towards histamine. HADH is a homodimer, with each 76 kDa subunit containing two redox cofactors: a [4Fe-4S] cluster and an unusual covalently bound flavin mononucleotide, 6-S-cysteinyl-FMN. In order to understand the substrate specificity of HADH, it was sought to determine its structure by X-ray crystallography. This enzyme has been expressed recombinantly in Escherichia coli and successfully crystallized in two forms. Diffraction data were collected to 2.7 {angstrom} resolution at the SSRL synchrotron with 99.7% completeness. The crystals belonged to the orthorhombic space group P2{sub 1}2{sub 1}2{sub 1}, with unit-cell parameters a = 101.14, b = 107.03, c = 153.35 {angstrom}.
- Authors:
- Publication Date:
- Research Org.:
- SLAC National Accelerator Lab., Menlo Park, CA (United States)
- Sponsoring Org.:
- USDOE
- OSTI Identifier:
- 953059
- Report Number(s):
- SLAC-REPRINT-2009-225
TRN: US0902667
- DOE Contract Number:
- AC02-76SF00515
- Resource Type:
- Journal Article
- Journal Name:
- Acta Crystallogr.F Struc.Biol.Crystalliz.Commun.64:785,2008
- Additional Journal Information:
- Journal Volume: 64; Journal Issue: 9
- Country of Publication:
- United States
- Language:
- English
- Subject:
- 43 PARTICLE ACCELERATORS; ACETALDEHYDE; CRYSTALLIZATION; CRYSTALLOGRAPHY; DEAMINATION; DIFFRACTION; ENZYMES; ESCHERICHIA COLI; HISTAMINE; IMIDAZOLES; ISOALLOXAZINES; OXIDOREDUCTASES; PURIFICATION; RESOLUTION; SPACE GROUPS; SPECIFICITY; SUBSTRATES; SYNCHROTRONS; Other,OTHER, BIO
Citation Formats
Reed, T M, Hirakawa, H, Mure, M, Scott, E E, and Limburg, J. Expression, Purification, Crystallization And Preliminary X-Ray Studies of Histamine Dehydrogenase From Nocardioides Simplex. United States: N. p., 2009.
Web.
Reed, T M, Hirakawa, H, Mure, M, Scott, E E, & Limburg, J. Expression, Purification, Crystallization And Preliminary X-Ray Studies of Histamine Dehydrogenase From Nocardioides Simplex. United States.
Reed, T M, Hirakawa, H, Mure, M, Scott, E E, and Limburg, J. 2009.
"Expression, Purification, Crystallization And Preliminary X-Ray Studies of Histamine Dehydrogenase From Nocardioides Simplex". United States.
@article{osti_953059,
title = {Expression, Purification, Crystallization And Preliminary X-Ray Studies of Histamine Dehydrogenase From Nocardioides Simplex},
author = {Reed, T M and Hirakawa, H and Mure, M and Scott, E E and Limburg, J},
abstractNote = {Histamine dehydrogenase (HADH) from Nocardioides simplex catalyzes the oxidative deamination of histamine to produce imidazole acetaldehyde and an ammonium ion. HADH is functionally related to trimethylamine dehydrogenase (TMADH), but HADH has strict substrate specificity towards histamine. HADH is a homodimer, with each 76 kDa subunit containing two redox cofactors: a [4Fe-4S] cluster and an unusual covalently bound flavin mononucleotide, 6-S-cysteinyl-FMN. In order to understand the substrate specificity of HADH, it was sought to determine its structure by X-ray crystallography. This enzyme has been expressed recombinantly in Escherichia coli and successfully crystallized in two forms. Diffraction data were collected to 2.7 {angstrom} resolution at the SSRL synchrotron with 99.7% completeness. The crystals belonged to the orthorhombic space group P2{sub 1}2{sub 1}2{sub 1}, with unit-cell parameters a = 101.14, b = 107.03, c = 153.35 {angstrom}.},
doi = {},
url = {https://www.osti.gov/biblio/953059},
journal = {Acta Crystallogr.F Struc.Biol.Crystalliz.Commun.64:785,2008},
number = 9,
volume = 64,
place = {United States},
year = {Thu May 21 00:00:00 EDT 2009},
month = {Thu May 21 00:00:00 EDT 2009}
}