The dapE-encoded N-Succinyl-L,L-Diaminopimelic Acid Desuccinylase from Haemophilus influenzae Is a Dinuclear Metallohydrolase

Nathaniel J. Cosper, David L. Bienvenue, Jacob E. Shokes, Danuta M. Gilner, Takashi Tsukamoto, Robert A. Scott, Richard C. Holz

Research output: Contribution to journalArticle

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.

Original languageEnglish (US)
Pages (from-to)14654-14655
Number of pages2
JournalJournal of the American Chemical Society
Volume125
Issue number48
DOIs
StatePublished - Dec 3 2003
Externally publishedYes

Fingerprint

Diaminopimelic Acid
Haemophilus influenzae
X ray absorption
X-Rays
Acids
Enzymes
Catalytic Domain
Fourier Analysis
Fourier transforms
X rays

ASJC Scopus subject areas

  • Chemistry(all)

Cite this

The dapE-encoded N-Succinyl-L,L-Diaminopimelic Acid Desuccinylase from Haemophilus influenzae Is a Dinuclear Metallohydrolase. / Cosper, Nathaniel J.; Bienvenue, David L.; Shokes, Jacob E.; Gilner, Danuta M.; Tsukamoto, Takashi; Scott, Robert A.; Holz, Richard C.

In: Journal of the American Chemical Society, Vol. 125, No. 48, 03.12.2003, p. 14654-14655.

Research output: Contribution to journalArticle

Cosper, Nathaniel J. ; Bienvenue, David L. ; Shokes, Jacob E. ; Gilner, Danuta M. ; Tsukamoto, Takashi ; Scott, Robert A. ; Holz, Richard C. / The dapE-encoded N-Succinyl-L,L-Diaminopimelic Acid Desuccinylase from Haemophilus influenzae Is a Dinuclear Metallohydrolase. In: Journal of the American Chemical Society. 2003 ; Vol. 125, No. 48. pp. 14654-14655.
@article{377c702cfe424672b436fe0048f20e9e,
title = "The dapE-encoded N-Succinyl-L,L-Diaminopimelic Acid Desuccinylase from Haemophilus influenzae Is a Dinuclear Metallohydrolase",
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 {\AA}, which can be fit for both [Zn_(DapE)] and [ZnZn(DapE)], assuming ca. 5 (N,O) scatterers at 1.96 and 1.98 {\AA}, respectively. A second-shell feature at ca. 3.34 {\AA} 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.",
author = "Cosper, {Nathaniel J.} and Bienvenue, {David L.} and Shokes, {Jacob E.} and Gilner, {Danuta M.} and Takashi Tsukamoto and Scott, {Robert A.} and Holz, {Richard C.}",
year = "2003",
month = "12",
day = "3",
doi = "10.1021/ja036650v",
language = "English (US)",
volume = "125",
pages = "14654--14655",
journal = "Journal of the American Chemical Society",
issn = "0002-7863",
publisher = "American Chemical Society",
number = "48",

}

TY - JOUR

T1 - The dapE-encoded N-Succinyl-L,L-Diaminopimelic Acid Desuccinylase from Haemophilus influenzae Is a Dinuclear Metallohydrolase

AU - Cosper, Nathaniel J.

AU - Bienvenue, David L.

AU - Shokes, Jacob E.

AU - Gilner, Danuta M.

AU - Tsukamoto, Takashi

AU - Scott, Robert A.

AU - Holz, Richard C.

PY - 2003/12/3

Y1 - 2003/12/3

N2 - 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.

AB - 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.

UR - http://www.scopus.com/inward/record.url?scp=0345293205&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0345293205&partnerID=8YFLogxK

U2 - 10.1021/ja036650v

DO - 10.1021/ja036650v

M3 - Article

VL - 125

SP - 14654

EP - 14655

JO - Journal of the American Chemical Society

JF - Journal of the American Chemical Society

SN - 0002-7863

IS - 48

ER -