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Activity of Select Dehydrogenases With Sepharose-Immobilized N(6)-carboxymethyl-NAD

Activity of Select Dehydrogenases With Sepharose-Immobilized N(6)-carboxymethyl-NAD

Justin Beauchamp, Claire Vieille

Bioengineered. 2015;6(2):106-10.

PMID: 25611453

Abstract:

N(6)-carboxymethyl-NAD (N(6)-CM-NAD) can be used to immobilize NAD onto a substrate containing terminal primary amines. We previously immobilized N(6)-CM-NAD onto sepharose beads and showed that Thermotoga maritima glycerol dehydrogenase could use the immobilized cofactor with cofactor recycling. We now show that Saccharomyces cerevisiae alcohol dehydrogenase, rabbit muscle L-lactate dehydrogenase (type XI), bovine liver L-glutamic dehydrogenase (type III), Leuconostoc mesenteroides glucose-6-phosphate dehydro-genase, and Thermotoga maritima mannitol dehydrogenase are active with soluble N(6)-CM-NAD. The products of all enzymes but 6-phospho-D-glucono-1,5-lactone were formed when sepharose-immobilized N(6)-CM-NAD was recycled by T. maritima glycerol dehydrogenase, indicating that N(6)-immobilized NAD is suitable for use by a variety of different dehydrogenases. Observations of the enzyme active sites suggest that steric hindrance plays a greater role in limiting or allowing activity with the modified cofactor than do polarity and charge of the residues surrounding the N(6)-amine group on NAD.

Chemicals Related in the Paper:

Catalog Number	Product Name	Structure	CAS Number	Price
AP9029123-A	L-Glutamic Dehydrogenase from bovine liver		9029-12-3	Price

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