Values CatLog read from this paper
The X-ray crystal structures of human alpha-phosphomannomutase 1 reveal the structural basis of congenital disorder of glycosylation type 1a
PMID 16540464doi:10.1074/jbc.m601505200Open in Browse
The paper itself is not on this site: read it at the publisher. This page lists only the values CatLog read from it.
CatLog read 4 records (12 values) from this paper: α-phosphomannomutase 1 (α-PMM1), α-phosphomannomutase 2 (α-PMM2) from Homo sapiens.
Read from the paper by an AI model and checked against the paper by a second, separate AI run; code converted the units. Values are in CatLog's units; each record opens in Browse with the line the paper prints and the checks.
| Enzyme | Organism | Substrate | kcat (s⁻¹) | Km (mM) | kcat/Km (mM⁻¹ s⁻¹) | Conditions | Open record |
|---|---|---|---|---|---|---|---|
| α-phosphomannomutase 1 (α-PMM1) | Homo sapiens | alpha-D-glucose 1-phosphate | 2.85 | 0.0075 | 380 | pH 6.5, 25 °C | Open record: α-phosphomannomutase 1 (α-PMM1), alpha-D-glucose 1-phosphate |
| α-phosphomannomutase 1 (α-PMM1) | Homo sapiens | alpha-D-mannose 1-phosphate | 4.39 | 0.054 | 81 | pH 6.5, 25 °C | Open record: α-phosphomannomutase 1 (α-PMM1), alpha-D-mannose 1-phosphate |
| α-phosphomannomutase 2 (α-PMM2) | Homo sapiens | alpha-D-glucose 1-phosphate | 1.72 | 0.0135 | 130 | pH 6.5, 25 °C | Open record: α-phosphomannomutase 2 (α-PMM2), alpha-D-glucose 1-phosphate |
| α-phosphomannomutase 2 (α-PMM2) | Homo sapiens | alpha-D-mannose 1-phosphate | 3.9 | 0.016 | 250 | pH 6.5, 25 °C | Open record: α-phosphomannomutase 2 (α-PMM2), alpha-D-mannose 1-phosphate |