Abstract
3,6-Anhydro-l-galactonate cycloisomerase (ACI), which is found in the marine bacterium Vibrio sp. strain EJY3, converts 3,6-anhydro-l-galactonate into 2-keto-3-deoxygalactonate. ACI is a key enzyme in the metabolic pathway of 3,6-anhydro-l-galactose (AHG). Study of AHG metabolism is important for the efficient fermentation of agar and biofuel production, because AHG is a sugar that is non-fermentable by commercial microorganisms. The aci gene from Vibrio sp. strain EJY3 was cloned, and the recombinant protein was overexpressed and crystallized in order to determine the structure and understand the function of the protein. The crystals diffracted to 2.2 Å resolution and belonged to space group P41212 or P43212, with unit-cell parameters a = b = 87.9, c = 143.5 Å. The Matthews coefficient was 2.3 Å3 Da-1, with a solvent content of 47%.3,6-Anhydro-l-galactonate cycloisomerase (ACI) is a second-step enzyme in the metabolic pathway of 3,6-anhydro-l-galactose. Structural analysis of ACI is crucial in order to elucidate its function, substrate specificity and reaction mechanism at the molecular level.
Original language | English |
---|---|
Pages (from-to) | 511-514 |
Number of pages | 4 |
Journal | Acta Crystallographica Section:F Structural Biology Communications |
Volume | 73 |
Issue number | 9 |
DOIs | |
Publication status | Published - 2017 Sept |
Bibliographical note
Publisher Copyright:© 2017 International Union of Crystallography.
Keywords
- 3,6-anhydro-l-galactonate
- 3,6-anhydro-l-galactonate cycloisomerase
- 3,6-anhydro-l-galactose
- ACI
- AHG metabolism
- AHGA
- Vibrio
- agarolytic pathway
ASJC Scopus subject areas
- Biophysics
- Structural Biology
- Biochemistry
- Genetics
- Condensed Matter Physics