Literature summary for 2.4.1.37 extracted from

Weissbach, S.; Fluegge, F.; Peters, T.
Substrate binding drives active-site closing of human blood group B balactosyltransferase as revealed by hot-spot labeling and NMR spectroscopy experiments (2018), ChemBioChem, 19, 970-978 .

Crystallization (Commentary)

Crystallization (Comment)	Organism
study of substrate-induced conformational transitions of GTB. Acceptor binding is fast on the chemical-shift timescale with rather small chemical-shift perturbations in the range of less than approximately 20 Hz. Donor or acceptor binding to GTB saturated with acceptor or donor substrate, respectively, is slow (below 10 Hz). Substrate binding drives the enzyme into the closed state required for catalysis	Homo sapiens

Crystallization (Comment)

Organism

study of substrate-induced conformational transitions of GTB. Acceptor binding is fast on the chemical-shift timescale with rather small chemical-shift perturbations in the range of less than approximately 20 Hz. Donor or acceptor binding to GTB saturated with acceptor or donor substrate, respectively, is slow (below 10 Hz). Substrate binding drives the enzyme into the closed state required for catalysis

Homo sapiens

Organism

Organism	UniProt	Comment	Textmining
Homo sapiens	P16442	-	-

Source Tissue

Source Tissue	Comment	Organism	Textmining

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)