A new class EC 7, Translocases, has been added to the EC list. It will be part of ENZYME from release 2018_10. Read more about EC 7 here.
ENZYME entry: EC 22.214.171.124
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|UDP-alpha-D-glucose + glycogenin <=> UDP + alpha-D-glucosylglycogenin|
- The first reaction of this enzyme is to catalyze its own
glucosylation, normally at a specific Tyr of the protein if this
group is free; when the Tyr is replaced by Thr or Phe, the enzyme's
self-glucosylation activity is lost but its intermolecular
transglucosylation ability remains.
- It continues to glucosylate an existing glucosyl group until a length
of about 5-13 residues has been formed.
- Further lengthening of the glycogen chain is then carried out by
- Not highly specific for the donor, using UDP-xylose in addition to
UDP-glucose (although not glucosylating or xylosylating a xylosyl
group so added).
- It can also use CDP-glucose and TDP-glucose, but not ADP-glucose or
- Similarly it is not highly specific for the acceptor, using water
(i.e. hydrolyzing UDP-glucose) among others.
- Various forms of the enzyme exist, and different forms predominate in
- Thus primate liver contains glycogenin-2, of molecular mass 66 kDa,
whereas the more widespread form is glycogenin-1, with a molecular
mass of 38 kDa.
- Formerly EC 126.96.36.199.
|PRIAM enzyme-specific profiles||188.8.131.52|
|KEGG Ligand Database for Enzyme Nomenclature||184.108.40.206|
|IUBMB Enzyme Nomenclature||220.127.116.11|
|MEDLINE||Find literature relating to 18.104.22.168|
|A7A018, GLG1_YEAS7; ||P36143, GLG1_YEAST; ||A6ZQJ2, GLG2_YEAS7; |
|P47011, GLG2_YEAST; ||O15488, GLYG2_HUMAN; ||P46976, GLYG_HUMAN; |
|Q9R062, GLYG_MOUSE; ||P13280, GLYG_RABIT; ||O08730, GLYG_RAT; |
|H2KYQ5, GYG1_CAEEL; |
entries corresponding to 2.4.1.-
All ENZYME / UniProtKB/Swiss-Prot entries corresponding to 2.4.-.-
All ENZYME / UniProtKB/Swiss-Prot entries corresponding to 2.-.-.-