|
type |
Journal Article |
authors |
Ford, G. C.; Eichele, G.; Jansonius, J. N. |
title |
Three-dimensional structure of a pyridoxal-phosphate-dependent enzyme, mitochondrial aspartate aminotransferase |
journal |
Proc Natl Acad Sci U S A |
Activity |
2.6.1.1 |
Family |
2.6.1.1.a |
PLP Fold Type |
1 |
ui |
80234662 |
year |
(1980) |
volume |
77 |
number |
5 |
pages |
2559-63. |
| |
keywords |
Animal |
abstract |
X-ray diffraction studies to 2.8-A resolution have yielded the three- dimensional structure of mitochondrial aspartate aminotransferase (L- aspartate:2-oxoglutarate aminotransferase, EC 2.6.1.1), an isologous alpha 2 dimer (Mr = 2 x 45,000). The subunits are rich in secondary structure and contain two domains, one of which anchors the coenzyme, pyridoxal 5'-phosphate. Each active site lies between the subunits and is composed of residues from both of them. |
last changed |
2014/03/03 17:48 |
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