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2.4.1.141: N-acetylglucosaminyldiphosphodolichol N-acetylglucosaminyltransferase

This is an abbreviated version!
For detailed information about N-acetylglucosaminyldiphosphodolichol N-acetylglucosaminyltransferase, go to the full flat file.

Word Map on EC 2.4.1.141

Reaction

UDP-N-acetyl-alpha-D-glucosamine
+
N-acetyl-alpha-D-glucosaminyl-diphosphodolichol
=
UDP
+
N-acetyl-beta-D-glucosaminyl-(1->4)-N-acetyl-alpha-D-glucosaminyl-diphosphodolichol

Synonyms

Alg 14, Alg13, Alg13p, Alg13p/Alg14p, Alg14, chitobiosyl-PP-lipid synthase, CLS, N,N'-diacetylchitobiosylpyrophosphoryldolichol synthase, UDP-GlcNAc transferase, UDP-GlcNAc:dolichyl-pyrophosphoryl-GlcNAc GlcNAc transferase, UDP-GlcNAc:GlcNAc-P-P-Dol N-acetylglucosaminyltransferase, uridine diphosphoacetylglucosamine-dolichylacetylglucosamine pyrophosphate acetylglucosaminyltransferase

ECTree

     2 Transferases
         2.4 Glycosyltransferases
             2.4.1 Hexosyltransferases
                2.4.1.141 N-acetylglucosaminyldiphosphodolichol N-acetylglucosaminyltransferase

General Stability

General Stability on EC 2.4.1.141 - N-acetylglucosaminyldiphosphodolichol N-acetylglucosaminyltransferase

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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
cytosolic Alg13p is very short-lived, whereas membrane-associated Alg13 is relatively stable. Cytosolic Alg13p is a target for proteasomal degradation, and the failure to degrade excess Alg13p leads to glycosylation defects. Alg13p degradation requires a C-terminal domain whose deletion results in Alg13p stability. Appending this sequence onto normally long-lived beta-galactosidase causes it to undergo rapid degradation, demonstrating that this C-terminal domain represents a novel and autonomous degradation motif. Proteasomal degradation of excess unassembled Alg13p is an important quality control mechanism that ensures proper protein complex assembly and correct N-linked glycosylation
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