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TitleStructural and kinetic studies on adenylosuccinate lyase from Mycobacterium smegmatis and Mycobacterium tuberculosis provide new insights on the catalytic residues of the enzyme.
Journal, issue, pagesFebs J., Vol. 281, Page 1642-1658, Year 2014
Publish dateNov 14, 2013 (structure data deposition date)
AuthorsBanerjee, S. / Agrawal, M.J. / Mishra, D. / Sharan, S. / Balaram, H. / Savithri, H.S. / Murthy, M.R.
External linksFebs J. / PubMed:24479855
MethodsX-ray diffraction
Resolution2.16 Å
Structure data

PDB-4nle:
Crystal structure of apo Adenylosuccinate Lyase from Mycobacterium smegmatis
Method: X-RAY DIFFRACTION / Resolution: 2.16 Å

Chemicals

ChemComp-HOH:
WATER

Source
  • mycobacterium smegmatis (bacteria)
KeywordsLYASE / Purine biosynthesis / purine salvage pathway / homotetramer / catalysis / aspartase/fumarase superfamily

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