Glyoxalase I from Brassica juncea is a calmodulin stimulated protein

Deswal, Renu ; Sopory, Sudhir Kumar (1999) Glyoxalase I from Brassica juncea is a calmodulin stimulated protein Biochimica et Biophysica Acta (BBA) - Molecular Cell Research, 1450 (3). pp. 460-467. ISSN 0167-4889

Full text not available from this repository.

Official URL:

Related URL:


Brassica juncea glyoxalase I (S-lactoylglutathione-lyase, EC is a 56 kDa, heterodimeric protein. It requires magnesium (Mg2+) for its optimal activity. In this report we provide biochemical evidence for modulation of glyoxalase I activity by calcium/calmodulin (Ca2+/CaM). In the presence of Ca2+ glyoxalase I showed a significant (2.6-fold) increase in its activity. It also showed a Ca2+ dependent mobility shift on denaturing gels. Its Ca2+ binding was confirmed by Chelex-100 assay and gel overlays using 45CaCl2. Glyoxalase I was activated by over 7-fold in the presence of Ca2+ (25 μM) and CaM (145 nM) and this stimulation was blocked by the CaM antibodies and a CaM inhibitor, trifluroperazine (150 µM). Glyoxalase I binds to a CaM-Sepharose column and was eluted by EGTA. The eluted protein fractions also showed stimulation by CaM. The stimulation of glyoxalase I activity by CaM was maximum in the presence of Mg2+ and Ca2+; however, magnesium alone also showed glyoxalase I activation by CaM.

Item Type:Article
Source:Copyright of this article belongs to Elsevier Science.
Keywords:Brassica juncea; Calcium and Calmodulin Binding; Isoform; Stress Signal Transduction
ID Code:49882
Deposited On:21 Jul 2011 09:29
Last Modified:21 Jul 2011 09:29

Repository Staff Only: item control page