Literature summary for 2.4.1.144 extracted from

Ihara, H.; Ikeda, Y.; Koyota, S.; Endo, T.; Honke, K.; Taniguchi, N.
A catalytically inactive beta1,4-N-acetylglucosaminyltransferase III (GnT-III) behaves as a dominant negative GnT-III inhibitor (2002), Eur. J. Biochem., 269, 193-201.

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Activating Compound

Activating Compound	Comment	Organism	Structure
Triton X-100	-	Homo sapiens
Triton X-100	-	Rattus norvegicus

Cloned(Commentary)

Cloned (Comment)	Organism
expression of a catalytically inactive D232A mutant in human hepatoblastoma cell line Huh6, leading to suppression of the endogenous enzyme activity, but not to a significant decrease in the expression level of the endogenous enzyme	Rattus norvegicus
expression of wild-type and mutants in COS-1 cells	Rattus norvegicus

Protein Variants

Protein Variants	Comment	Organism
D321A	site-directed mutagenesis, expression level in COS-1 cells similar to wild-type, but no remaining catalytic activity	Rattus norvegicus
D323A	site-directed mutagenesis, expression level in COS-1 cells similar to wild-type, but no remaining catalytic activity	Rattus norvegicus
D323A	expression of a catalytically inactive D232A mutant in human hepatoblastoma cell line Huh6, leading to suppression of the endogenous enzyme activity, but not to a significant decrease in the expression level of the endogenous enzyme	Rattus norvegicus
D329A	site-directed mutagenesis, unaltered compared to wild-type	Rattus norvegicus

Inhibitors

Inhibitors	Comment	Organism	Structure
inactive rat mutant D323A enzyme	acts as an inhibitor of endogenous enzyme activity when expressed in human Huh6 cells	Homo sapiens

Metals/Ions

Metals/Ions	Comment	Organism	Structure
Mn2+	-	Homo sapiens
Mn2+	Asp321 and Asp323 are absolutely required for the coordination of Mn2+ during enzyme reaction	Rattus norvegicus

Organism

Organism	UniProt	Comment	Textmining
Homo sapiens	-	-	-
Rattus norvegicus	-	-	-

Posttranslational Modification

Posttranslational Modification	Comment	Organism
glycoprotein	3 N-glycosylation sites: Asn243, Asn261, Asn399, essential for activity, tunicamycin-treated enzyme, which is not glycosylated, shows no activity	Rattus norvegicus

Source Tissue

Source Tissue	Comment	Organism	Textmining
HuH-6 cell	hepatoblastoma cell line	Homo sapiens	-

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg]	Specific Activity Maximum [µmol/min/mg]	Comment	Organism
0.000017	-	wild-type and mutant D329A	Rattus norvegicus

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
UDP-N-acetyl-D-glucosamine + (N-acetyl-beta-D-glucosaminyl-1,2-alpha-D-mannosyl-1,3)-(N-acetyl-beta-D-glucosaminyl-1,2-alpha-D-mannosyl-1,6)-beta-D-mannosyl-1,4-N-acetyl-beta-D-glucosaminyl-R	-	Homo sapiens	UDP + N-acetyl-beta-D-glucosaminyl-1,2-alpha-D-mannosyl-1,3-(N-acetyl-beta-D-glucosaminyl-1,2-alpha-D-mannosyl-1,6)-(N-acetyl-beta-D-glucosaminyl-1,4)-beta-D-mannosyl-1,4-N-acetyl-beta-D-glucosaminyl-R	incorporates a N-acetylglucosamine residue in beta-1,4-linkage to beta-linked mannosyl, i.e. bisecting N-acetylglucosamine	?
UDP-N-acetyl-D-glucosamine + (N-acetyl-beta-D-glucosaminyl-1,2-alpha-D-mannosyl-1,3)-(N-acetyl-beta-D-glucosaminyl-1,2-alpha-D-mannosyl-1,6)-beta-D-mannosyl-1,4-N-acetyl-beta-D-glucosaminyl-R	absolute requirement for the conserved residues Asp321 and Asp323 as part of a D-X-D motif	Rattus norvegicus	UDP + N-acetyl-beta-D-glucosaminyl-1,2-alpha-D-mannosyl-1,3-(N-acetyl-beta-D-glucosaminyl-1,2-alpha-D-mannosyl-1,6)-(N-acetyl-beta-D-glucosaminyl-1,4)-beta-D-mannosyl-1,4-N-acetyl-beta-D-glucosaminyl-R	incorporates a N-acetylglucosamine residue in beta-1,4-linkage to beta-linked mannosyl, i.e. bisecting N-acetylglucosamine	?

Synonyms

Synonyms	Comment	Organism
beta1,4-N-acetylglucosaminyltransferase III	-	Homo sapiens
beta1,4-N-acetylglucosaminyltransferase III	-	Rattus norvegicus
GnT-III	-	Homo sapiens
GnT-III	-	Rattus norvegicus

pH Optimum

pH Optimum Minimum	pH Optimum Maximum	Comment	Organism
6.3	-	assay at	Homo sapiens
6.3	-	assay at	Rattus norvegicus

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Release 2023.1 (January 2023)