Deciphering the number and location of active sites in the monomeric glyoxalase I of Zea mays
Detoxification of methylglyoxal, a toxic by-product of central sugar metabolism, is a major issue for all forms of life. The glyoxalase pathway evolved to effectively convert methylglyoxal into D-lactate via a glutathione hemithioacetal intermediate. Recently, we have shown that the monomeric glyoxa...
Guardado en:
| Autores principales: | , , , , , |
|---|---|
| Formato: | article artículo |
| Lenguaje: | Inglés |
| Publicado: |
Wiley
2022
|
| Materias: | |
| Acceso en línea: | http://hdl.handle.net/2133/23461 http://hdl.handle.net/2133/23461 |
| Aporte de: |
| id |
I15-R121-2133-23461 |
|---|---|
| record_format |
dspace |
| institution |
Universidad Nacional de Rosario |
| institution_str |
I-15 |
| repository_str |
R-121 |
| collection |
Repositorio Hipermedial de la Universidad Nacional de Rosario (UNR) |
| language |
Inglés |
| orig_language_str_mv |
eng |
| topic |
Glyoxalase I Hemithioacetal Maize Methylglyoxal Protein tunnel |
| spellingShingle |
Glyoxalase I Hemithioacetal Maize Methylglyoxal Protein tunnel Gonzalez, Javier M. Agostini, Romina B. Alvarez, Clarisa Ester Klinke, Sebastián Andreo, Carlos S. Campos Bermudez, Valeria A. Deciphering the number and location of active sites in the monomeric glyoxalase I of Zea mays |
| topic_facet |
Glyoxalase I Hemithioacetal Maize Methylglyoxal Protein tunnel |
| description |
Detoxification of methylglyoxal, a toxic by-product of central sugar metabolism, is a major issue for all forms of life. The glyoxalase pathway evolved to effectively convert methylglyoxal into D-lactate via a glutathione hemithioacetal intermediate. Recently, we have shown that the monomeric glyoxalase I from maize exhibits a symmetric fold with two cavities, potentially harboring two active sites, in analogy with homodimeric enzyme surrogates. Here we confirm that only one of the two cavities exhibits glyoxalase I activity and show that it adopts a tunnel-shaped structure upon substrate binding. Such conformational change gives rise to independent binding sites for glutathione and methylglyoxal in the same active site, with important implications for the molecular reaction mechanism, which has been a matter of debate for several decades. |
| format |
article artículo |
| author |
Gonzalez, Javier M. Agostini, Romina B. Alvarez, Clarisa Ester Klinke, Sebastián Andreo, Carlos S. Campos Bermudez, Valeria A. |
| author_facet |
Gonzalez, Javier M. Agostini, Romina B. Alvarez, Clarisa Ester Klinke, Sebastián Andreo, Carlos S. Campos Bermudez, Valeria A. |
| author_sort |
Gonzalez, Javier M. |
| title |
Deciphering the number and location of active sites in the monomeric glyoxalase I of Zea mays |
| title_short |
Deciphering the number and location of active sites in the monomeric glyoxalase I of Zea mays |
| title_full |
Deciphering the number and location of active sites in the monomeric glyoxalase I of Zea mays |
| title_fullStr |
Deciphering the number and location of active sites in the monomeric glyoxalase I of Zea mays |
| title_full_unstemmed |
Deciphering the number and location of active sites in the monomeric glyoxalase I of Zea mays |
| title_sort |
deciphering the number and location of active sites in the monomeric glyoxalase i of zea mays |
| publisher |
Wiley |
| publishDate |
2022 |
| url |
http://hdl.handle.net/2133/23461 http://hdl.handle.net/2133/23461 |
| work_keys_str_mv |
AT gonzalezjavierm decipheringthenumberandlocationofactivesitesinthemonomericglyoxalaseiofzeamays AT agostinirominab decipheringthenumberandlocationofactivesitesinthemonomericglyoxalaseiofzeamays AT alvarezclarisaester decipheringthenumberandlocationofactivesitesinthemonomericglyoxalaseiofzeamays AT klinkesebastian decipheringthenumberandlocationofactivesitesinthemonomericglyoxalaseiofzeamays AT andreocarloss decipheringthenumberandlocationofactivesitesinthemonomericglyoxalaseiofzeamays AT camposbermudezvaleriaa decipheringthenumberandlocationofactivesitesinthemonomericglyoxalaseiofzeamays |
| bdutipo_str |
Repositorios |
| _version_ |
1764820412147957763 |