Glyoxalase II from A. thaliana requires Zn(II) for catalytic activity.
FEBS Lett
; 418(3): 351-4, 1997 Dec 01.
Article
en En
| MEDLINE
| ID: mdl-9428743
Cytosolic glyoxalase II from Arabidopsis thaliana, GLX2-2, was overexpressed and purified to homogeneity using Q-sepharose chromatography. MALDI-TOF mass spectrometry studies indicated a molecular weight of 28 767 Da. Using steady-state kinetics studies, the purified enzyme exhibited a Km of 660 +/- 100 microM and a kcat of 484 +/- 92 s(-1) at 37 degrees C. Metal analyses demonstrated that the enzyme binds 2.1 +/- 0.5 moles of Zn(II) per monomer; the binding of Zn(II) is essential for enzyme viability and activity. Sequence comparison of glyoxalase II enzymes from human, A. thaliana, and yeast and the metallo-beta-lactamases reveal that all metal binding ligands of the metallo-beta-lactamases are conserved in glyoxalase II enzymes, suggesting that all glyoxalase II enzymes are Zn(II) metalloenzymes. These results and their implications are discussed in light of previous studies on glyoxalase II, and an active site for the glyoxalase II enzymes is proposed.
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Colección:
01-internacional
Base de datos:
MEDLINE
Asunto principal:
Tioléster Hidrolasas
/
Arabidopsis
Límite:
Humans
Idioma:
En
Revista:
FEBS Lett
Año:
1997
Tipo del documento:
Article
País de afiliación:
Estados Unidos
Pais de publicación:
Reino Unido