digitonin and 2-4-diacetamido-2-4-6-trideoxyglucopyranose

digitonin has been researched along with 2-4-diacetamido-2-4-6-trideoxyglucopyranose* in 1 studies

Other Studies

1 other study(ies) available for digitonin and 2-4-diacetamido-2-4-6-trideoxyglucopyranose

Article	Year
Structure of the external aldimine form of PglE, an aminotransferase required for N,N'-diacetylbacillosamine biosynthesis. Protein science : a publication of the Protein Society, 2015, Volume: 24, Issue:10 N,N'-diacetylbacillosamine is a novel sugar that plays a key role in bacterial glycosylation. Three enzymes are required for its biosynthesis in Campylobacter jejuni starting from UDP-GlcNAc. The focus of this investigation, PglE, catalyzes the second step in the pathway. It is a PLP-dependent aminotransferase that converts UDP-2-acetamido-4-keto-2,4,6-trideoxy-d-glucose to UDP-2-acetamido-4-amino-2,4,6-trideoxy-d-glucose. For this investigation, the structure of PglE in complex with an external aldimine was determined to a nominal resolution of 2.0 Å. A comparison of its structure with those of other sugar aminotransferases reveals a remarkable difference in the manner by which PglE accommodates its nucleotide-linked sugar substrate. Topics: Acetylglucosamine; Campylobacter jejuni; Carbohydrate Sequence; Crystallography, X-Ray; Digitonin; Lysine; Semicarbazides; Transaminases; Valine	2015

Article

Year

Structure of the external aldimine form of PglE, an aminotransferase required for N,N'-diacetylbacillosamine biosynthesis.

Protein science : a publication of the Protein Society, 2015, Volume: 24, Issue:10

N,N'-diacetylbacillosamine is a novel sugar that plays a key role in bacterial glycosylation. Three enzymes are required for its biosynthesis in Campylobacter jejuni starting from UDP-GlcNAc. The focus of this investigation, PglE, catalyzes the second step in the pathway. It is a PLP-dependent aminotransferase that converts UDP-2-acetamido-4-keto-2,4,6-trideoxy-d-glucose to UDP-2-acetamido-4-amino-2,4,6-trideoxy-d-glucose. For this investigation, the structure of PglE in complex with an external aldimine was determined to a nominal resolution of 2.0 Å. A comparison of its structure with those of other sugar aminotransferases reveals a remarkable difference in the manner by which PglE accommodates its nucleotide-linked sugar substrate.

Topics: Acetylglucosamine; Campylobacter jejuni; Carbohydrate Sequence; Crystallography, X-Ray; Digitonin; Lysine; Semicarbazides; Transaminases; Valine

2015