7P75

Re-engineered 2-deoxy-D-ribose-5-phosphate aldolase catalysing asymmetric Michael addition reactions in substrate-free state

This is a non-PDB format compatible entry.

Summary for 7P75

• Entry DOI: 10.2210/pdb7p75/pdb
• Descriptor: Deoxyribose-phosphate aldolase (2 entities in total)
• Functional Keywords: protein engineering, directed evolution, dera, aldolase, carboligase, michael addition, carbon-carbon lyase, lyase
• Biological source: Escherichia coli (strain ATCC 8739 / DSM 1576 / NBRC 3972 / NCIMB 8545 / WDCM 00012 / Crooks)
• Total number of polymer chains: 2
• Total formula weight: 57367.48

Authors

Thunnissen, A.M.W.H.,Rozeboom, H.J.,Kunzendorf, A.,Poelarends, G.J. (deposition date: 2021-07-19, release date: 2021-10-27, Last modification date: 2024-01-31)

• Primary citation: Kunzendorf, A.,Xu, G.,van der Velde, J.J.H.,Rozeboom, H.J.,Thunnissen, A.W.H.,Poelarends, G.J.; Unlocking Asymmetric Michael Additions in an Archetypical Class I Aldolase by Directed Evolution.; Acs Catalysis, 11:13236-13243, 2021; PubMed: 34765282; DOI: 10.1021/acscatal.1c03911

Experimental method

X-RAY DIFFRACTION (1.23 Å)