EC Number   |
General Information |
Reference |
|---|
    6.3.2.1 | malfunction |
alanine mutation of the catalytic sites of pantothenate synthetase causes distinct conformational changes in the ATP binding region. Analysis of the molecular mechanism of decreased affinity of the enzyme for ATP caused by alanine mutations using molecular dynamics simulations and free energy calculations |
-, 746489 |
| 6.3.2.1 | metabolism |
the pantothenate synthetase is involved in the pantothenate biosynthetic pathway |
-, 745786 |
| 6.3.2.1 | more |
significance and importance of conserved active site residues including His44, His47, Asn69, Gln72, Lys160 and Gln164 in substrate binding and formation of pantoyl adenylate intermediate. Molecular dynamics simulations of enzyme PS-ATP complex, substrate binding pocket and residue interactions analysis |
-, 746489 |
| 6.3.2.1 | physiological function |
pantothenate synthetase catalyzes the ATP-dependent formation of an amide bond between pantoate and beta-alanine |
-, 744723 |
| 6.3.2.1 | physiological function |
pantothenate synthetase, an enzyme that is involved in the pantothenate biosynthetic pathway, is essential for the virulence and persistent growth of Mycobacterium tuberculosis |
-, 745786 |
| 6.3.2.1 | physiological function |
the pantothenate biosynthetic pathway is essential for the persistent growth and virulence of Mycobacterium tuberculosis and one of the enzymes in the pathway |
-, 744725 |
