Biology Reference
In-Depth Information
Figure 3.16
Plausible pathway in phosphorylase-catalyzed
N
-formyl-
α
-
glucosaminylation of Glc
.
5
the molecular masses of pentasaccharide-octasaccharide containing
a GlcNF unit. This finding indicated the occurrence of both the
N
-formyl-
α
-glucosaminylation by GlcNF-1-P and
α
-glucosylation
by Glc-1-P when Glc
was used as a glycosyl acceptor (Fig. 3.16).
5
Because Glc
is the smallest substrate for phosphorolysis in the
presence of inorganic phosphate, Glc-1-P was possibly produced by
phosphorolysis of Glc
5
at the
early stage of the reaction, where inorganic phosphate was formed
by the transfer of a GlcNF unit from GlcNF-1-P to Glc
with simultaneous production of Glc
5
4
. Then, Glc-1-P
was recognized more efficiently by phosphorylase than GlcNF-1-P.
Thus, the maltooligosaccharides with larger DPs, such as Glc
5
and
6
Glc
, were produced by the transfer of the glucose residue from Glc-
1-P to Glc
7
-glucosaminylation of
the produced maltooligosaccharides by GlcNF-1-P proceeded once,
subsequent glycosylation was suppressed because the
or Glc
. Furthermore, if
N
-formyl-
α
4
5
-
glucosaminylated oligosaccharides were less efficiently recognized
by phosphorylase.
N
-formyl-
α
References
1. Kitaoka, M., and Hayashi, K. (2002). Carbohydrate-processing
phosphorolytic enzymes,
, pp. 35-50.
2. Seibel, J., Jördening, H.-J., and Buchholz, K. (2006). Glycosylation with
activated sugars using glycosyltransferases and transglycosidases,
Biocatal. Biotranform
Trends Glycosci. Glycotechnol.
,
14
.,
24
, pp. 311-342.
