Photolabeling of dextransucrase from Streptococcus sanguis with p-azidophenyl alpha-D-glucopyranoside.
Dextransucrase from Streptococcus sanguis ATCC 10558 was photolabeled using p-azidophenyl alpha-D-glucopyranoside with an apparent rate constant of inactivation of 1.40 min-1. The dissociation constant for this compound, which acts as an acceptor molecule in the enzymatic reaction, is 90 microM. Apparently two acceptor binding sites exist on dextransucrase as shown by (i.) photolabeling the enzyme with p-azidophenyl-alpha-D-[5,6-3H]glucopyranoside and (ii.) fluorescence titration experiments.
Kobs
S F
SF
Department of Chemistry, Ohio State University, Columbus 43210.
Mayer
R M
RM
D000345:Affinity Labels; D001386:Azides; D001665:Binding Sites; D002240:Carbohydrate Sequence; D005960:Glucosides; D005964:Glucosyltransferases / Q000737:chemistry*; D007700:Kinetics; D008969:Molecular Sequence Data; D015394:Molecular Structure; D010777:Photochemistry; D013298:Streptococcus sanguis / Q000201:enzymology*; D014466:Ultraviolet Rays
D000345:Affinity Labels; D001386:Azides; D005960:Glucosides; C072303:4-azidophenylglucopyranoside; D005964:Glucosyltransferases; C020025:dextransucrase