EC Number |
Cofactor |
Reference |
---|
4.2.1.20 | more |
the alpha-subunit contains no prosthetic group |
649237 |
4.2.1.20 | pyridoxal 5'-phosphate |
- |
5548, 5556, 5565, 5567, 649903, 649979, 650081, 650441, 652086, 652118, 652475, 658339, 677838, 678240, 678297, 678298, 678399, 679080, 679191, 680462, 681414, 681986, 682470, 701445, 716453 |
4.2.1.20 | pyridoxal 5'-phosphate |
2 mol bound per mol of beta2 subunit |
5550 |
4.2.1.20 | pyridoxal 5'-phosphate |
crystal structures of apo-beta2 and holo-beta2 from Escherichia coli is determined at 3.0 and 2.9 A resolutions. The apo-type and holo-type molecule retain a dimeric form in solution. The subunit structures of both the apo-beta2 and the holo-beta2 forms consist of two domains, (N domain, C domain). The pyridoxal 5'-phosphate-bound holo-form has multiple interactions between the two domains and a long loop (residues 260-310), which are missing in the apo-form |
703681 |
4.2.1.20 | pyridoxal 5'-phosphate |
dependent |
678168 |
4.2.1.20 | pyridoxal 5'-phosphate |
dependent on |
649898, 649899, 650222, 650304, 650403, 650850, 651955, 729099 |
4.2.1.20 | pyridoxal 5'-phosphate |
dependent on, bound to the enzyme |
652899 |
4.2.1.20 | pyridoxal 5'-phosphate |
dependent on, bound via Schiff base to beta-subunit residue Lys87 |
652550 |
4.2.1.20 | pyridoxal 5'-phosphate |
dependent on, His86 is necessary for binding and stabilization in a correct orientation in the active site of the beta-subunit |
651967 |
4.2.1.20 | pyridoxal 5'-phosphate |
forms a Schiff base with the epsilon amino-group of Lys87 |
5567 |