Degradation of Derivatives of N-Acetyl-D-glucosamine by Rhodococcus rhodochrous IFO 15564: Substrate Specificity and Its Application to the Synthesis of Allyl α-N-Acetyl-D-glucosaminide

A Kuboki; R Komiya; T Sekiguchi; K Katsuragi; T Sugai; H Ohta

doi:10.1271/bbb.62.1581

Degradation of Derivatives of N-Acetyl-D-glucosamine by Rhodococcus rhodochrous IFO 15564: Substrate Specificity and Its Application to the Synthesis of Allyl α-N-Acetyl-D-glucosaminide

Biosci Biotechnol Biochem. 1998;62(8):1581-5. doi: 10.1271/bbb.62.1581.

Authors

A Kuboki¹, R Komiya¹, T Sekiguchi¹, K Katsuragi¹, T Sugai¹, H Ohta¹

Affiliation

¹ a Department of Chemistry, Keio University.

PMID: 27388842
DOI: 10.1271/bbb.62.1581

Abstract

The substrate specificity was studied for the metabolic degradation of N-acetyl-D-glucosamine (GlcNAc) derivatives by Rhodococcus rhodochrous IFO 15564 which possesses N-acetyl-D-glucosamine deacetylase as a key-step enzyme. This microorganism degraded a wide range of substrates with modified N-acyl groups. The metabolizing activity of this strain became low to the substrates substituted at 1,3,4,6-positions of GlcNAc, and GlcNAc itself was suggested to be metabolized via an open-chain aldehyde form. Based on these results, a simplified procedure for the isolation of allyl α-N-acetyl-D-glucosaminide from an α, β-anomeric mixture was developed by selectively hydrolyzing the β-anomer with Jackbean β-N-acetyl-D-glucosaminidase and subsequently degrading the resulting N-acetyl-D-glucosamine in the reaction mixture with this microorganism.

Keywords: N-acetyl-D-glucosamine; N-acetyl-D-glucosamine deacetylase; Rhodococcus rhodochrous IFO 15564; allyl α-N-acetyl-D-glucosaminide; β-N-acetyl-D-glucosaminidase.