Literature summary for 2.6.1.104 extracted from

van Straaten, K.E.; Ko, J.B.; Jagdhane, R.; Anjum, S.; Palmer, D.R.; Sanders, D.A.
The structure of NtdA, a sugar aminotransferase involved in the kanosamine biosynthetic pathway in Bacillus subtilis, reveals a new subclass of aminotransferases (2013), J. Biol. Chem., 288, 34121-34130.

Search for more literature for 2.6.1.104

Cloned(Commentary)

Cloned (Comment)	Organism
expression in Escherichia coli	Bacillus subtilis

Crystallization (Commentary)

Crystallization (Comment)	Organism
enzyme shares the common type 1 aspartate aminotransferase fold with residues from both monomers forming the active site. The structure of the enzyme alone reveals the internal aldimine form of NtdA with the cofactor pyridoxal phosphate covalently attached to Lys247. The addition of glutamate results in formation of pyridoxamine phosphate. Co-crystallization with kanosamine 6-phosphate results in the formation of the external aldimine. Only alpha-D-kanosamine 6-phosphate is observed in the active site of NtdA, not the beta-anomer	Bacillus subtilis

Crystallization (Comment)

Organism

enzyme shares the common type 1 aspartate aminotransferase fold with residues from both monomers forming the active site. The structure of the enzyme alone reveals the internal aldimine form of NtdA with the cofactor pyridoxal phosphate covalently attached to Lys247. The addition of glutamate results in formation of pyridoxamine phosphate. Co-crystallization with kanosamine 6-phosphate results in the formation of the external aldimine. Only alpha-D-kanosamine 6-phosphate is observed in the active site of NtdA, not the beta-anomer

Bacillus subtilis

Organism

Organism	UniProt	Comment	Textmining
Bacillus subtilis	O07566	-	-

Synonyms

Synonyms	Comment	Organism
3-oxo-glucose-6-phosphate:glutamate aminotransferase	-	Bacillus subtilis
ntdA	-	Bacillus subtilis

Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.

Release 2023.1 (January 2023)