The dapE-encoded N-Succinyl-l,l-Diaminopimelic Acid Desuccinylase from Haemophilus influenzae Is a Dinuclear Metallohydrolase
Document Type
Article
Language
eng
Format of Original
2 p.
Publication Date
12-3-2003
Publisher
American Chemical Society
Source Publication
Journal of the American Chemical Society
Source ISSN
0002-7863
Original Item ID
DOI: 10.1021/ja036650v
Abstract
The Zn K-edge extended X-ray absorption fine structure (EXAFS) spectra, of the dapE-encoded N-succinyl-l,l-diaminopimelic acid desuccinylase (DapE) from Haemophilus influenzae have been recorded in the presence of one or two equivalents of Zn(II) (i.e. [Zn_(DapE)] and [ZnZn(DapE)]). The Fourier transforms of the Zn EXAFS are dominated by a peak at ca. 2.0 Å, which can be fit for both [Zn_(DapE)] and [ZnZn(DapE)], assuming ca. 5 (N,O) scatterers at 1.96 and 1.98 Å, respectively. A second-shell feature at ca. 3.34 Å appears in the [ZnZn(DapE)] EXAFS spectrum but is significantly diminished in [Zn_(DapE)]. These data show that DapE contains a dinuclear Zn(II) active site. Since no X-ray crystallographic data are available for any DapE enzyme, these data provide the first glimpse at the active site of DapE enzymes. In addition, the EXAFS data for DapE incubated with two competitive inhibitors, 2-carboxyethylphosphonic acid and 5-mercaptopentanoic acid, are also presented.
Recommended Citation
Cosper, Nathaniel J.; Bienvenue, David L.; Shokes, Jacob E.; Gilner, Danuta M.; Tsukamoto, Takashi; Scott, Robert A.; and Holz, Richard C., "The dapE-encoded N-Succinyl-l,l-Diaminopimelic Acid Desuccinylase from Haemophilus influenzae Is a Dinuclear Metallohydrolase" (2003). Chemistry Faculty Research and Publications. 314.
https://epublications.marquette.edu/chem_fac/314
Comments
Accepted version. Journal of the American Chemical Society, Vol. 125, No. 48 (December 3, 2003): 14654-14655. DOI. © 2003 American Chemical Society. Used with permission.
Richard C. Holz was affiliated with Utah State University at the time of publication.