Literature summary for 5.4.2.3 extracted from

Nishitani, Y.; Maruyama, D.; Nonaka, T.; Kita, A.; Fukami, T.A.; Mio, T.; Yamada-Okabe, H.; Yamada-Okabe, T.; Miki, K.
Crystal structures of N-acetylglucosamine-phosphate mutase, a member of the alpha-D-phosphohexomutase superfamily, and its substrate and product complexes (2006), J. Biol. Chem., 281, 19740-19747.

Crystallization (Commentary)

Crystallization (Comment)	Organism
both in apo form and in the complex forms with substrate and product. Protein consists of four domains. of which three domains have essentially the same fold. The catalytic cleft is formed by four loops from each domains. The N-acetyl group of the substrate is recognized by V370 and N389 in domain 3, from which the substrate specificity arises. Substrate rotates about 180° on the axis linking C4 and the midpoint of the C5-O5 bond in the reaction	Candida albicans

Crystallization (Comment)

Organism

both in apo form and in the complex forms with substrate and product. Protein consists of four domains. of which three domains have essentially the same fold. The catalytic cleft is formed by four loops from each domains. The N-acetyl group of the substrate is recognized by V370 and N389 in domain 3, from which the substrate specificity arises. Substrate rotates about 180° on the axis linking C4 and the midpoint of the C5-O5 bond in the reaction

Candida albicans

Organism

Organism	UniProt	Comment	Textmining
Candida albicans	Q9P4V2	-	-

Reaction

Reaction	Comment	Organism	Reaction ID
N-acetyl-alpha-D-glucosamine 1-phosphate = N-acetyl-D-glucosamine 6-phosphate	the N-acetyl group of the substrate is recognized by V370 and N389 in domain 3, from which the substrate specificity arises. Substrate rotates about 180° on the axis linking C4 and the midpoint of the C5-O5 bond in the reaction	Candida albicans	a

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)