EC Number |
Substrates |
Organism |
Products |
Reversibility |
---|
2.4.1.142 | GDP-alpha-D-mannose + chitobiosyldiphosphodolichol |
- |
Sus scrofa |
GDP + beta-(1->4)-D-mannosylchitobiosyldiphosphodolichol |
- |
? |
2.4.1.142 | GDP-alpha-D-mannose + chitobiosyldiphosphodolichol |
- |
Glycine max |
GDP + beta-(1->4)-D-mannosylchitobiosyldiphosphodolichol |
- |
? |
2.4.1.142 | GDP-alpha-D-mannose + chitobiosyldiphosphodolichol |
- |
Homo sapiens |
GDP + beta-(1->4)-D-mannosylchitobiosyldiphosphodolichol |
- |
? |
2.4.1.142 | GDP-alpha-D-mannose + diphosphodolichyl-N-acetyl-D-glucosaminyl-N-acetyl-D-glucosamine |
- |
Homo sapiens |
GDP + beta-(1->4)-D-mannosylchitobiosyl diphosphodolichol |
- |
? |
2.4.1.142 | GDP-alpha-D-mannose + N-acetyl-beta-D-glucosaminyl-(1->4)-N-acetyl-alpha-D-glucosaminyl-diphosphodolichol |
- |
Homo sapiens |
GDP + beta-D-mannosyl-(1->4)-N-acetyl-beta-D-glucosaminyl-(1->4)-N-acetyl-alpha-D-glucosaminyl-diphosphodolichol |
- |
? |
2.4.1.142 | GDP-alpha-D-mannose + N-acetyl-beta-D-glucosaminyl-(1->4)-N-acetyl-alpha-D-glucosaminyl-diphosphodolichol |
- |
Saccharomyces cerevisiae |
GDP + beta-D-mannosyl-(1->4)-N-acetyl-beta-D-glucosaminyl-(1->4)-N-acetyl-alpha-D-glucosaminyl-diphosphodolichol |
- |
? |
2.4.1.142 | GDP-alpha-D-mannose + N-acetyl-beta-D-glucosaminyl-(1->4)-N-acetyl-alpha-D-glucosaminyl-diphosphodolichol |
- |
Rattus norvegicus |
GDP + beta-D-mannosyl-(1->4)-N-acetyl-beta-D-glucosaminyl-(1->4)-N-acetyl-alpha-D-glucosaminyl-diphosphodolichol |
- |
? |
2.4.1.142 | GDP-alpha-D-mannose + N-acetyl-beta-D-glucosaminyl-(1->4)-N-acetyl-alpha-D-glucosaminyl-diphosphodolichol |
- |
Saccharomyces cerevisiae ATCC 204508 |
GDP + beta-D-mannosyl-(1->4)-N-acetyl-beta-D-glucosaminyl-(1->4)-N-acetyl-alpha-D-glucosaminyl-diphosphodolichol |
- |
? |
2.4.1.142 | more |
patient with congenital disorder of glycosylation is compound heterozygous for three mutations in the ALG1 gene, leading to the amino acid substitutions S150R and D429E on one allele and S258L on the other. The detrimental effect of these mutations on ALG1 protein function is demonstrated in a complementation assay. This novel type of congenital disorder of glycosylation should be referred to as CDG-Ik |
Homo sapiens |
? |
- |
? |
2.4.1.142 | more |
the molecular nature of severe multisystemic disorder with a recurrent nonimmune hydrops fetalis is identified as deficiency of GDP-Man:GlcNAc2-PP-dolichol mannosyltransferase caused by a C773T transition |
Homo sapiens |
? |
- |
? |