KEGG   ENZYME: 2.4.1.144Help
Entry
EC 2.4.1.144                Enzyme                                 

Name
beta-1,4-mannosyl-glycoprotein 4-beta-N-acetylglucosaminyltransferase;
N-acetylglucosaminyltransferase III;
N-glycosyl-oligosaccharide-glycoprotein N-acetylglucosaminyltransferase III;
uridine diphosphoacetylglucosamine-glycopeptide beta4-acetylglucosaminyltransferase III;
beta-1,4-mannosyl-glycoprotein beta-1,4-N-acetylglucosaminyltransferase;
GnTIII;
GlcNAc-T III;
MGAT3 (gene name);
UDP-N-acetyl-D-glucosamine:beta-D-mannosyl-glycoprotein 4-beta-N-acetyl-D-glucosaminyltransferase
Class
Transferases;
Glycosyltransferases;
Hexosyltransferases
BRITE hierarchy
Sysname
UDP-N-acetyl-alpha-D-glucosamine:beta-D-mannosyl-glycoprotein 4-beta-N-acetyl-D-glucosaminyltransferase (configuration-inverting)
Reaction(IUBMB)
UDP-N-acetyl-alpha-D-glucosamine + beta-D-GlcNAc-(1->2)-alpha-D-Man-(1->3)-[beta-D-GlcNAc-(1->2)-alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-beta-D-GlcNAc-N-Asn-[protein] = UDP + beta-D-GlcNAc-(1->2)-alpha-D-Man-(1->3)-[beta-D-GlcNAc-(1->2)-alpha-D-Man-(1->6)]-[beta-D-GlcNAc-(1->4)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-beta-D-GlcNAc-N-Asn-[protein] [RN:R05986]
Reaction(KEGG)
R05986(G);
(other) R07259
Show
Substrate
UDP-N-acetyl-alpha-D-glucosamine [CPD:C00043];
beta-D-GlcNAc-(1->2)-alpha-D-Man-(1->3)-[beta-D-GlcNAc-(1->2)-alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-beta-D-GlcNAc-N-Asn-[protein]
Product
UDP [CPD:C00015];
beta-D-GlcNAc-(1->2)-alpha-D-Man-(1->3)-[beta-D-GlcNAc-(1->2)-alpha-D-Man-(1->6)]-[beta-D-GlcNAc-(1->4)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-beta-D-GlcNAc-N-Asn-[protein]
Comment
The enzyme, found in vertebrates, participates in the processing of N-glycans in the Golgi apparatus. The residue added by the enzyme at position 4 of the beta-linked mannose of the trimannosyl core of N-glycans is known as a bisecting GlcNAc. Unlike GlcNAc residues added to other positions, it is not extended or modified. In addition, its presence prevents the action of other branching enzymes involved in the process such as GlcNAc-T IV (EC 2.4.1.145) and GlcNAc-T V (EC 2.4.1.155), and thus increased activity of GlcNAc-T III leads to a decrease in highly branched N-glycan structures.
History
EC 2.4.1.144 created 1984, modified 2001 (EC 2.4.1.51 created 1972, part incorporated 1984), modified 2018
Pathway
ec00510  N-Glycan biosynthesis
ec01100  Metabolic pathways
Orthology
K00737  beta-1,4-mannosyl-glycoprotein beta-1,4-N-acetylglucosaminyltransferase
Genes
HSA: 4248(MGAT3)
PTR: 470218(MGAT3)
PPS: 100986687(MGAT3)
GGO: 101140166(MGAT3)
PON: 100461728(MGAT3)
NLE: 100587045(MGAT3)
MCC: 703643(MGAT3)
MCF: 102119319(MGAT3)
CSAB: 103223343(MGAT3)
RRO: 104682561(MGAT3)
RBB: 108520473(MGAT3)
CJC: 100401747(MGAT3)
SBQ: 101041876(MGAT3)
MMU: 17309(Mgat3)
RNO: 29582(Mgat3)
CGE: 100689076(Mgat3)
NGI: 103748565(Mgat3)
HGL: 101726123(Mgat3)
CCAN: 109692650(Mgat3)
OCU: 100339892(MGAT3) 100355590
TUP: 102479156(MGAT3)
CFA: 481244(MGAT3)
AML: 100484334(MGAT3)
UMR: 103676517(MGAT3)
ORO: 101368902(MGAT3)
FCA: 101096819(MGAT3)
PTG: 102951185(MGAT3)
AJU: 106979885(MGAT3)
BTA: 520087(MGAT3)
BOM: 102272014(MGAT3)
BIU: 109559830(MGAT3)
PHD: 102326943(MGAT3)
CHX: 102185445(MGAT3)
OAS: 101123204(MGAT3)
SSC: 100625969(MGAT3)
CFR: 102511595(MGAT3)
CDK: 105091930(MGAT3)
BACU: 103016283(MGAT3)
LVE: 103083856(MGAT3)
OOR: 101282927(MGAT3)
ECB: 100055333(MGAT3)
EPZ: 103565286(MGAT3)
EAI: 106842433(MGAT3)
MYB: 102245140(MGAT3)
MYD: 102751860(MGAT3)
HAI: 109392246(MGAT3)
RSS: 109448831(MGAT3)
PALE: 102897210(MGAT3)
LAV: 100660621(MGAT3)
TMU: 101344852
MDO: 100012345(MGAT3)
SHR: 100917350(MGAT3)
OAA: 100090777(MGAT3)
GGA: 418013(MGAT3)
MGP: 100550573(MGAT3)
CJO: 107312706(MGAT3)
APLA: 101794219(MGAT3)
ACYG: 106035842(MGAT3)
TGU: 100226352(MGAT3)
GFR: 102036532(MGAT3)
FAB: 101814927(MGAT3)
PHI: 102100315(MGAT3)
PMAJ: 107205069(MGAT3)
CCAE: 111934874(MGAT3)
CCW: 104696331(MGAT3)
FPG: 101921320(MGAT3)
FCH: 102048799(MGAT3)
CLV: 102093513(MGAT3)
EGZ: 104134240(MGAT3)
AAM: 106488447(MGAT3)
ASN: 102370976(MGAT3)
AMJ: 102563722(MGAT3)
PSS: 102450203(MGAT3)
CMY: 102941302(MGAT3)
CPIC: 101950417(MGAT3)
ACS: 100564985(mgat3)
PVT: 110088077(MGAT3)
PBI: 103058421(MGAT3)
GJA: 107117145(MGAT3)
XLA: 108714526 108715764(mgat3.S)
XTR: 100492491(mgat3)
NPR: 108799496(MGAT3)
DRE: 553676(mgat3a) 570828(mgat3b)
IPU: 108272883(mgat3) 108272992(Mgat3)
AMEX: 103038268(mgat3)
TRU: 101062954(mgat3)
LCO: 104925458(mgat3) 109136945
NCC: 104942929(mgat3)
MZE: 101485628(mgat3)
OLA: 101173368(mgat3)
XMA: 102221250(mgat3)
PRET: 103461029 103478406(mgat3)
NFU: 107375157(mgat3)
KMR: 108230131(mgat3)
CSEM: 103383418(mgat3)
LCF: 108889054(mgat3)
SDU: 111235861(mgat3)
HCQ: 109511269(mgat3)
BPEC: 110156010 110157727(mgat3)
MALB: 109975050(mgat3)
ELS: 105029655 105031194(mgat3)
SFM: 108928829(mgat3) 108930685
LCM: 102355106(MGAT3) 102367673
CMK: 103172616(mgat3)
DME: Dmel_CG31849(CG31849)
DER: 6543130
DPE: 6602241
DSI: Dsimw501_GD22083(Dsim_GD22083)
DWI: 6641793
MDE: 101895677
AAG: 5566942
AME: 100578875
BIM: 100742613
BTER: 100645675
SOC: 105204601
AEC: 105154063
ACEP: 105617964
PBAR: 105428492
HST: 105190563
DQU: 106750769
CFO: 105257864
LHU: 105672181
PGC: 109856918
PCF: 106792036
NVI: 100680240
MDL: 103577860
TCA: 103312582
DPA: 109533323
NVL: 108565977
ZNE: 110828324
LJA: Lj1g3v3688880.1(Lj1g3v3688880.1) Lj1g3v3688880.2(Lj1g3v3688880.2) Lj2g3v0921530.1(Lj2g3v0921530.1) Lj4g3v1881510.1(Lj4g3v1881510.1) Lj4g3v2731600.1(Lj4g3v2731600.1) Lj6g3v0528360.1(Lj6g3v0528360.1)
DOSA: Os02t0594900-01(Os02g0594900) Os02t0595100-01(Os02g0595100) Os04t0477500-01(Os04g0477500) Os12t0611900-01(Os12g0611900)
ATS: 109735745(LOC109735745) 109736375(LOC109736375) 109758585(LOC109758585) 109773322(LOC109773322) 109781560(LOC109781560)
NCR: NCU07455
NTE: NEUTE1DRAFT125174(NEUTE1DRAFT_125174)
MGR: MGG_04516
SSCK: SPSK_03420
MAW: MAC_00259
MBE: MBM_00251
ABP: AGABI1DRAFT112787(AGABI1DRAFT_112787)
ABV: AGABI2DRAFT192752(AGABI2DRAFT_192752)
ENC: ECL_01461
ECLO: ENC_12120
ECLX: LI66_10060
ECLZ: LI64_10215
BCEW: DM40_2963
BMU: Bmul_0967
BMJ: BMULJ_02297(mgaT)
BUB: BW23_1298
BLAT: WK25_11290
BGO: BM43_1837
BGP: BGL_1c03960(mgaT)
PNU: Pnuc_1802
PNE: Pnec_0274
BBA: Bd1672
BBAT: Bdt_1662
BBAC: EP01_04540
PSF: PSE_3293
RCE: RC1_4017
TMO: TMO_a0549
BPB: bpr_I2522
BHU: bhn_I2388
FLM: MY04_2799
 » show all
Taxonomy
Reference
1  [PMID:6213618]
  Authors
Narasimhan S.
  Title
Control of glycoprotein synthesis. UDP-GlcNAc:glycopeptide beta 4-N-acetylglucosaminyltransferase III, an enzyme in hen oviduct which adds GlcNAc in beta 1-4 linkage to the beta-linked mannose of the trimannosyl core of N-glycosyl oligosaccharides.
  Journal
J Biol Chem 257:10235-42 (1982)
Reference
2  [PMID:6366476]
  Authors
Schachter H, Narasimhan S, Gleeson P, Vella G.
  Title
Glycosyltransferases involved in elongation of N-glycosidically linked oligosaccharides of the complex or N-acetyllactosamine type.
  Journal
Methods Enzymol 98:98-134 (1983)
Reference
3  [PMID:2975180]
  Authors
Brockhausen I, Carver JP, Schachter H
  Title
Control of glycoprotein synthesis. The use of oligosaccharide substrates and HPLC to study the sequential pathway for N-acetylglucosaminyltransferases I, II, III,  IV, V, and VI in the biosynthesis of highly branched N-glycans by hen oviduct membranes.
  Journal
Biochem Cell Biol 66:1134-51 (1988)
Reference
4  [PMID:1325461]
  Authors
Nishikawa A, Ihara Y, Hatakeyama M, Kangawa K, Taniguchi N
  Title
Purification, cDNA cloning, and expression of UDP-N-acetylglucosamine: beta-D-mannoside beta-1,4N-acetylglucosaminyltransferase III from rat kidney.
  Journal
J Biol Chem 267:18199-204 (1992)
  Sequence
[rno:29582]
Reference
5  [PMID:8370666]
  Authors
Ihara Y, Nishikawa A, Tohma T, Soejima H, Niikawa N, Taniguchi N
  Title
cDNA cloning, expression, and chromosomal localization of human N-acetylglucosaminyltransferase III (GnT-III).
  Journal
J Biochem 113:692-8 (1993)
  Sequence
[hsa:4248]
Other DBs
ExplorEnz - The Enzyme Database: 2.4.1.144
IUBMB Enzyme Nomenclature: 2.4.1.144
ExPASy - ENZYME nomenclature database: 2.4.1.144
BRENDA, the Enzyme Database: 2.4.1.144
CAS: 83744-93-8

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