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Literature summary extracted from
- The X-ray crystal structures of human alpha-phosphomannomutase 1 reveal the structural basis of congenital disorder of glycosylation type 1a (2006), J. Biol. Chem., 281, 14918-14926.
Application
| EC Number | Application | Comment | Organism |
|---|---|---|---|
| 5.4.2.8 | medicine | analysis of clinically important mutations involved in congential disorder of glycosylation type 1a | Homo sapiens |
Crystallization (Commentary)
| EC Number | Crystallization (Comment) | Organism |
|---|---|---|
| 5.4.2.8 | isoform alpha-PMM1 in the open conformation, with and without bound substrate alpha-D-mannose 1-phosphate. Protein consists of two domains, the cap and the core. Substrate phosphate group is at a positively charged site of the cap domain, suggesting that substrate binds first to the cap and then is swept into the active site, thereby facilitating its closure over the core domain | Homo sapiens |
Protein Variants
| EC Number | Protein Variants | Comment | Organism |
|---|---|---|---|
| 5.4.2.8 | D188G | | mutant of isoform PMM2, 2% of wild-type activiy, involved in congential disorder of glycosylation type 1a | Homo sapiens |
| 5.4.2.8 | D65Y | mutant of isoform PMM2, involved in congential disorder of glycosylation type 1a | Homo sapiens |
| 5.4.2.8 | F119L | mutant of isoform PMM2, involved in congential disorder of glycosylation type 1a | Homo sapiens |
| 5.4.2.8 | R141H | mutant of isoform PMM2, 0.4% of wild-type activiy, involved in congential disorder of glycosylation type 1a | Homo sapiens |
| 5.4.2.8 | R162W | mutant of isoform PMM2, involved in congential disorder of glycosylation type 1a | Homo sapiens |
| 5.4.2.8 | V129M | mutant of isoform PMM2, involved in congential disorder of glycosylation type 1a | Homo sapiens |
| 5.4.2.8 | V231M | mutant of isoform PMM2, loss of stability at 40°C, involved in congential disorder of glycosylation type 1a | Homo sapiens |
KM Value [mM]
| EC Number | KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|---|
| 5.4.2.8 | 0.0075 | - |
D-glucose 1-phosphate | isoform alpha-PMM1, pH 6.5, 25°C | Homo sapiens |  |
| 5.4.2.8 | 0.0135 | - |
D-glucose-1-phosphate | isoform alpha-PMM2, pH 6.5, 25°C | Homo sapiens | |
| 5.4.2.8 | 0.016 | - |
D-mannose-1-phosphate | isoform alpha-PMM2, pH 6.5, 25°C | Homo sapiens | |
| 5.4.2.8 | 0.054 | - |
D-mannose 1-phosphate | isoform alpha-PMM1, pH 6.5, 25°C | Homo sapiens | |
Organism
| EC Number | Organism | UniProt | Comment | Textmining |
|---|---|---|---|---|
| 5.4.2.8 | Homo sapiens | O15305 | isoform alpha-PMM2 | - |
| 5.4.2.8 | Homo sapiens | Q92871 | isoform alpha-PMM1 | - |
Substrates and Products (Substrate)
| EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 5.4.2.8 | D-glucose 1-phosphate | - |
Homo sapiens | D-glucose 6-phosphate | - |
? | |
| 5.4.2.8 | D-glucose-1-phosphate | - |
Homo sapiens | D-glucose-6-phosphate | - |
? | |
| 5.4.2.8 | D-Mannose 1-phosphate | - |
Homo sapiens | D-Mannose 6-phosphate | - |
? | |
Turnover Number [1/s]
| EC Number | Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|---|
| 5.4.2.8 | 1.72 | - |
D-glucose-1-phosphate | isoform alpha-PMM2, pH 6.5, 25°C | Homo sapiens | |
| 5.4.2.8 | 2.85 | - |
D-glucose 1-phosphate | isoform alpha-PMM1, pH 6.5, 25°C | Homo sapiens | |
| 5.4.2.8 | 3.9 | - |
D-mannose-1-phosphate | isoform alpha-PMM2, pH 6.5, 25°C | Homo sapiens | |
| 5.4.2.8 | 4.4 | - |
D-mannose 1-phosphate | isoform alpha-PMM1, pH 6.5, 25°C | Homo sapiens | |
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