Abstract
l-Lactate oxidase (LOX) from Aerococcus viridans is a member of the α-hydroxyacid-oxidase flavoenzyme family. We have determined the three-dimensional structure of LOX and revealed the mechanism of substrate recognition. The LOX monomer structure has a typical α8/β8 motif commonly found in other flavin family proteins. A related enzyme, glycolate oxidase, catalyzes the oxidation of glycolate rather than lactate. Comparison of the two enzyme structures highlights the importance of five residues around the FMN prosthetic group of LOX, which act synergistically to discriminate between the l/d configurations of lactate. X-ray crystallography of LOX gave a space group I422 of unit-cell parameters a = b = 191.096 Å, c = 194.497 Å and α = β = γ = 90° with four monomers per asymmetric unit. The four independent monomers display slight structural differences around the active site. Diffraction data were collected, under cryogenic conditions to 2.1 Å resolution at the synchrotron facilities in Japan.
| Original language | English |
|---|---|
| Pages (from-to) | 249-256 |
| Number of pages | 8 |
| Journal | Biochemical and Biophysical Research Communications |
| Volume | 350 |
| Issue number | 2 |
| DOIs | |
| Publication status | Published - Nov 17 2006 |
| Externally published | Yes |
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Keywords
- Flavoprotein
- Lactate oxidase
- Substrate recognition
- X-ray structure analysis
ASJC Scopus subject areas
- Biochemistry
- Biophysics
- Molecular Biology
Cite this
The crystal structure of l-lactate oxidase from Aerococcus viridans at 2.1 Å resolution reveals the mechanism of strict substrate recognition. / Umena, Yasufumi; Yorita, Kazuko; Matsuoka, Takeshi; Kita, Akiko; Fukui, Kiyoshi; Morimoto, Yukio.
In: Biochemical and Biophysical Research Communications, Vol. 350, No. 2, 17.11.2006, p. 249-256.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - The crystal structure of l-lactate oxidase from Aerococcus viridans at 2.1 Å resolution reveals the mechanism of strict substrate recognition
AU - Umena, Yasufumi
AU - Yorita, Kazuko
AU - Matsuoka, Takeshi
AU - Kita, Akiko
AU - Fukui, Kiyoshi
AU - Morimoto, Yukio
PY - 2006/11/17
Y1 - 2006/11/17
N2 - l-Lactate oxidase (LOX) from Aerococcus viridans is a member of the α-hydroxyacid-oxidase flavoenzyme family. We have determined the three-dimensional structure of LOX and revealed the mechanism of substrate recognition. The LOX monomer structure has a typical α8/β8 motif commonly found in other flavin family proteins. A related enzyme, glycolate oxidase, catalyzes the oxidation of glycolate rather than lactate. Comparison of the two enzyme structures highlights the importance of five residues around the FMN prosthetic group of LOX, which act synergistically to discriminate between the l/d configurations of lactate. X-ray crystallography of LOX gave a space group I422 of unit-cell parameters a = b = 191.096 Å, c = 194.497 Å and α = β = γ = 90° with four monomers per asymmetric unit. The four independent monomers display slight structural differences around the active site. Diffraction data were collected, under cryogenic conditions to 2.1 Å resolution at the synchrotron facilities in Japan.
AB - l-Lactate oxidase (LOX) from Aerococcus viridans is a member of the α-hydroxyacid-oxidase flavoenzyme family. We have determined the three-dimensional structure of LOX and revealed the mechanism of substrate recognition. The LOX monomer structure has a typical α8/β8 motif commonly found in other flavin family proteins. A related enzyme, glycolate oxidase, catalyzes the oxidation of glycolate rather than lactate. Comparison of the two enzyme structures highlights the importance of five residues around the FMN prosthetic group of LOX, which act synergistically to discriminate between the l/d configurations of lactate. X-ray crystallography of LOX gave a space group I422 of unit-cell parameters a = b = 191.096 Å, c = 194.497 Å and α = β = γ = 90° with four monomers per asymmetric unit. The four independent monomers display slight structural differences around the active site. Diffraction data were collected, under cryogenic conditions to 2.1 Å resolution at the synchrotron facilities in Japan.
KW - Flavoprotein
KW - Lactate oxidase
KW - Substrate recognition
KW - X-ray structure analysis
UR - http://www.scopus.com/inward/record.url?scp=33749335515&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=33749335515&partnerID=8YFLogxK
U2 - 10.1016/j.bbrc.2006.09.025
DO - 10.1016/j.bbrc.2006.09.025
M3 - Article
C2 - 17007814
AN - SCOPUS:33749335515
VL - 350
SP - 249
EP - 256
JO - Biochemical and Biophysical Research Communications
JF - Biochemical and Biophysical Research Communications
SN - 0006-291X
IS - 2
ER -