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. Author manuscript; available in PMC: 2014 Mar 1.
Published in final edited form as: Crit Rev Biochem Mol Biol. 2012 Dec 19;48(2):10.3109/10409238.2012.745476. doi: 10.3109/10409238.2012.745476

Figure 9.

Figure 9

Selected KR structures and typical catalytic mechanism. (A) DEBS KR1 with cofactor binding, catalytic triads are shown as sticks. Blue: structural subdomain; Green: catalytic subdomain; Orange: “LDD” moiety shown as sticks. Magenta: Lid helix and loop. PDB code: 2FR0. (B) Different paths of entrance result in the different product stereochemistries in A and B type KRs. The presence of orange DLL loop in B-type KR will prevent substrate from entering behind the magenta lid. (C) Mechanism of KR catalyzed reduction. (D) Substrate-tuned stereoselectivity in Hpm8KR. 215×176mm (300 × 300 DPI).