Mechanistic study of the intramolecular conversion of maltose to trehalose by Thermus caldophilus GK24 trehalose synthase.
This paper questions what types of molecular transformation are involved in the conversion of maltose to trehalose by trehalose synthase from Thermus caldophilus GK24. The reverse reaction pathway has been examined with the aid of alpha,alpha-(2,4,6,6',2',4',6",6"'-(2)H(8))trehalose (1). The mass data of the isolated reaction products clearly indicate that deuterated glucose is confined only to substrate molecules, and thus the reversible enzymatic conversion of trehalose into maltose proceeds through an intramolecular pathway.
Koh
Sukhoon
S
Laboratory of Glycobiology, Korea Research Institute of Bioscience and Biotechnology, Daejeon, Republic of Korea.
Kim
Joongsu
J
Shin
Hyun-Jae
HJ
Lee
DuckHee
D
Bae
Jungdon
J
Kim
Dooil
D
Lee
Dae-Sil
DS
D004187:Disaccharides / Q000737:chemistry / Q000378:metabolism; D004926:Escherichia coli / Q000235:genetics; D005964:Glucosyltransferases / Q000235:genetics / Q000378:metabolism*; D009682:Magnetic Resonance Spectroscopy; D008320:Maltose / Q000737:chemistry / Q000378:metabolism*; D015394:Molecular Structure; D011994:Recombinant Proteins / Q000235:genetics / Q000302:isolation & purification / Q000378:metabolism; D021241:Spectrometry, Mass, Electrospray Ionization; D013824:Thermus / Q000201:enzymology* / Q000235:genetics; D013997:Time Factors; D014199:Trehalose / Q000737:chemistry / Q000378:metabolism*
D004187:Disaccharides; D011994:Recombinant Proteins; D008320:Maltose; D014199:Trehalose; D005964:Glucosyltransferases; C099692:trehalose synthase