KEGG   ENZYME: 2.4.1.186Help
Entry
EC 2.4.1.186                Enzyme                                 
Name
glycogenin glucosyltransferase;
glycogenin;
priming glucosyltransferase;
UDP-glucose:glycogenin glucosyltransferase
Class
Transferases;
Glycosyltransferases;
Hexosyltransferases
BRITE hierarchy
Sysname
UDP-alpha-D-glucose:glycogenin alpha-D-glucosyltransferase
Reaction(IUBMB)
UDP-alpha-D-glucose + glycogenin = UDP + alpha-D-glucosylglycogenin [RN:R03681]
Reaction(KEGG)
Substrate
UDP-alpha-D-glucose [CPD:C00029];
glycogenin [CPD:C01702]
Product
UDP [CPD:C00015];
alpha-D-glucosylglycogenin [CPD:C02687]
Comment
The first reaction of this enzyme is to catalyse its own glucosylation, normally at Tyr-194 of the protein if this group is free. When Tyr-194 is replaced by Thr or Phe, the enzyme's Mn2+-dependent self-glucosylation activity is lost but its intermolecular transglucosylation ability remains [7]. 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 EC 2.4.1.11, glycogen (starch) synthase. The enzyme is 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 GDP-glucose. Similarly it is not highly specific for the acceptor, using water (i.e. hydrolysing UDP-glucose) among others. Various forms of the enzyme exist, and different forms predominate in different organs. 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.
Orthology
K00750  
glycogenin glucosyltransferase
Genes
HSA: 
2992(GYG1) 8908(GYG2)
PTR: 
460765(GYG1) 465469(GYG2)
PPS: 
100977408(GYG1) 100995852(GYG2)
GGO: 
101130219(GYG1) 101153384(GYG2)
PON: 
100431369(GYG2) 100434629(GYG1)
MCC: 
712495(GYG1) 720568(GYG2)
MMU: 
27357(Gyg)
RNO: 
81675(Gyg1)
CFA: 
491717(GYG2) 611614(GYG1)
AML: 
FCA: 
101080946(GYG2) 101082176(GYG1)
BTA: 
280812(GYG1) 505258(GYG2)
SSC: 
100620160
ECB: 
100058811 100064536
MDO: 
100010174 100012580
SHR: 
100926747(GYG1) 100931311(GYG2)
OAA: 
100075592
GGA: 
418660(GYG2) 425050(GYG1)
MGP: 
100546787 100549941
TGU: 
100219874 100226558(GYG1)
ACS: 
100557488 100562212
XLA: 
100126641(gyg2) 446485(gyg1) 779133(gyg)
XTR: 
394883(gyg1) 496877(gyg2)
DRE: 
406831(gyg1a) 415152(gyg1b) 561803(gyg2)
TRU: 
101065299
OLA: 
101157097
BFO: 
BRAFLDRAFT_257976
CIN: 
100178599
SPU: 
754694
DME: 
Dmel_CG9480(Glycogenin)
DPO: 
Dpse_GA21819
DYA: 
Dyak_GE12180
CQU: 
CpipJ_CPIJ013596
AME: 
552421
NVI: 
100122700(NV11504)
API: 
100164266
ISC: 
IscW_ISCW006112
CEL: 
CELE_T25E12.5(gyg-2)
CBR: 
CBG13253 CBG14232(Cbr-uvt-5)
BMY: 
Bm1_16775
TSP: 
Tsp_05820
SMM: 
Smp_008490
NVE: 
NEMVE_v1g129041
HMG: 
100213497
TAD: 
TRIADDRAFT_30669
AQU: 
100635890
RCU: 
RCOM_0138290 RCOM_1590700
KLA: 
KLLA0A05709g
PPA: 
PAS_chr4_0847
DHA: 
DEHA2F17138g
PIC: 
PICST_76484(GLG2) PICST_86206(GLG1)
PGU: 
PGUG_04227
LEL: 
LELG_02698
CAL: 
CaO19.7434(GLG22)
CTP: 
CTRG_02219
CDU: 
CD36_86420
YLI: 
YALI0C21065g
CLU: 
CLUG_02358
NCR: 
NCU06698
PAN: 
PODANSg8384
NFI: 
NFIA_019190
CIM: 
CIMG_03907
URE: 
UREG_02029
MBR: 
MONBRDRAFT_1946
TGO: 
TGME49_110400
TVA: 
TVAG_014980
TPS: 
THAPSDRAFT_7435
 » show all
Taxonomy
Reference
1  [PMID:809265]
  Authors
Krisman CR, Barengo R.
  Title
A precursor of glycogen biosynthesis: alpha-1,4-glucan-protein.
  Journal
Eur. J. Biochem. 52 (1975) 117-23.
Reference
2  [PMID:3121316]
  Authors
Pitcher J, Smythe C, Campbell DG, Cohen P.
  Title
Identification of the 38-kDa subunit of rabbit skeletal muscle glycogen synthase as glycogenin.
  Journal
Eur. J. Biochem. 169 (1987) 497-502.
  Organism
Oryctolagus cuniculus
Reference
3  [PMID:2970965]
  Authors
Pitcher J, Smythe C, Cohen P.
  Title
Glycogenin is the priming glucosyltransferase required for the initiation of glycogen biogenesis in rabbit skeletal muscle.
  Journal
Eur. J. Biochem. 176 (1988) 391-5.
  Organism
Oryctolagus cuniculus
Reference
4
  Authors
Kennedy, L.D., Kirkman, B.R., Lomako, J., Rodriguez, I.R. and Whelan, W.J.
  Title
The biogenesis of rabbit-muscle glycogen.
  Journal
In: Berman, M.C. and Opie, L.A. (Eds.), Membranes and Muscle, ICSU Press/IRL Press, Oxford, 1985, p. 65-84.
Reference
5  [PMID:4062948]
  Authors
Rodriguez IR, Whelan WJ.
  Title
A novel glycosyl-amino acid linkage: rabbit-muscle glycogen is covalently linked to a protein via tyrosine.
  Journal
Biochem. Biophys. Res. Commun. 132 (1985) 829-36.
  Organism
Oryctolagus cuniculus
Reference
6  [PMID:2973423]
  Authors
Lomako J, Lomako WM, Whelan WJ.
  Title
A self-glucosylating protein is the primer for rabbit muscle glycogen biosynthesis.
  Journal
FASEB. J. 2 (1988) 3097-103.
  Organism
Oryctolagus cuniculus
Reference
7  [PMID:7797519]
  Authors
Alonso MD, Lomako J, Lomako WM, Whelan WJ.
  Title
Catalytic activities of glycogenin additional to autocatalytic self-glucosylation.
  Journal
J. Biol. Chem. 270 (1995) 15315-9.
  Organism
Oryctolagus cuniculus
Reference
8  [PMID:7672505]
  Authors
Alonso MD, Lomako J, Lomako WM, Whelan WJ.
  Title
A new look at the biogenesis of glycogen.
  Journal
FASEB. J. 9 (1995) 1126-37.
  Organism
Homo sapiens [GN:hsa], Oryctolagus cuniculus
Reference
9  [PMID:9857012]
  Authors
Mu J, Roach PJ.
  Title
Characterization of human glycogenin-2, a self-glucosylating initiator of liver glycogen metabolism.
  Journal
J. Biol. Chem. 273 (1998) 34850-6.
  Organism
Homo sapiens [GN:hsa]
Reference
10 [PMID:12051921]
  Authors
Gibbons BJ, Roach PJ, Hurley TD.
  Title
Crystal structure of the autocatalytic initiator of glycogen biosynthesis, glycogenin.
  Journal
J. Mol. Biol. 319 (2002) 463-77.
  Organism
Oryctolagus cuniculus
Other DBs
ExplorEnz - The Enzyme Database: 
IUBMB Enzyme Nomenclature: 
ExPASy - ENZYME nomenclature database: 
BRENDA, the Enzyme Database: 
CAS: 
117590-73-5
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