MINT MINT, Dpt of Biology, University of Rome Tor Vergata MINT http://mint.bio.uniroma2.it/mint url>http://mint.bio.uniroma2.it/mint/ https://mint.bio.uniroma2.it MINT-[0-9]+ https://mint.bio.uniroma2.it/index.php/results-interactions/?id=${ac} The Molecular INTeraction database (MINT) is a relational database designed to store interactions between biological molecules. http://mint.bio.uniroma2.it Structural and kinetic studies on Adenylosuccinate Lyase from Mycobacterium smegmatis and Mycobacterium tuberculosis provide new insights on the catalytic residues of the enzyme. Structural and kinetic studies on Adenylosuccinate Lyase from Mycobacterium smegmatis and Mycobacterium tuberculosis provide new insights on the catalytic residues of the enzyme. FEBS J. (1742-464X) 2014 imex curation Banerjee S., Agrawal M.J., Mishra D., Sharan S., Balaram H., Savithri H.S., Murthy M.R. mrn@mbu.iisc.ernet.in 18-Feb-2014: Contacted by IntAct-Help. Only protein-protein interactions in vitro In vitro x-ray diffraction x-ray crystallography X-ray X-ray x-ray diffraction predetermined predetermined participant predetermined mrn@mbu.iisc.ernet.in Accepted 2014-JAN-27 by LUANA 2014 imex curation a0r4i6_mycs2 Adenylosuccinate lyase purB Adenylosuccinase MSMEG_5847 protein protein mycs2 Mycobacterium smegmatis (strain ATCC 700084 / mc(2)155) MFVTIPNVLANRYASDEMVAIWSPEAKIIAERRLWLAVLRAQAELGVAVPDGVVEDYERVLENVDLESIAARERVTRHDVKARIEEFNALAGHEHVHKGMTSRDLTENVEQLQIRQSLELVFSHGVAVVARLAERAVVYRDLVMAGRSHNVAAQATTLGKRFASAAEETLVALTRLRELIDRYPLRGVKGPMGTAQDMLDLFGGDVGKLADLERRVAEFLGFTEVFTSVGQVYPRSLDHDVLSALVQFGAGPSSMAHTIRLMAGHELVTEGFAPGQVGSSAMPHKMNTRSCERVNGLQVVLRGYASMAAELAGAQWNEGDVFCSVVRRVALPDAFFAIDGQTETFLTVLDEFGAYPAVIQRELDRYLPFLATTRILMAAVRAGVGREAAHEVIKEHAVAVALAMREQGREPDLIDRLAGDPRLPLDKVALEAALEDKQAFTGAAGDQVDGVVAAVGELVSRYPEAAKYTSGAIL BBB24E11942F9807 purb-1 1 2 predetermined predetermined participant predetermined predetermined predetermined participant predetermined unspecified role unspecified role neutral component neutral component purified purified direct interaction direct interaction t1 f3 X-ray crystal structure of Mycobacterium smegmatis apo-adenylosuccinate lyase (ASL) with a partially ordered active site loop was determined at 2.16 Å resolution. The structure suggests that His149, Lys285 and Ser279 are functionally important. The low catalytic activity observed for M. smegmatis and M. tuberculosis ASLs is consistent with their slow growth rate