Backbone and Ile-δ1, Leu, Val methyl 1 H, 15 N, and 13 C, chemical shift assignments for Rhizopus chinensis lipase

Lipase r27RCL is a 296-residue, 33 kDa monomeric enzyme with high ester hydrolysis activity, which has significant applications in the baking, paper and leather industries. The lipase gene proRCL from Rhizopus microsporus var. chinensis (also Rhizopus chinensis ) CCTCC M201021 was cloned as a fusion construct C-terminal to a maltose-binding protein (MBP) tag, and expressed as MBP-proRCL in an Escherichia coli BL21 trxB (DE3) expression system with uniform 2 H, 13 C, 15 N-enrichment and Ile-δ1, Leu, and Val 13 CH 3 methyl labeling. The fusion protein was hydrolyzed by Kex2 protease at the recognition site Lys-Arg between residues −29 and −28 of the prosequence, producing the enzyme form called r27RCL. Here we report extensive backbone 1 H, 15 N, and 13 C, as well as Ile-δ1, Leu, and Val side chain methyl, NMR resonance assignments for r27RCL.