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 Atypical features of a Ure2p glutathione transferase from Phanerochaete chrysosporium. Atypical features of a Ure2p glutathione transferase from Phanerochaete chrysosporium. FEBS Lett. (0014-5793) 2013 Thuillier A., Roret T., Favier F., Gelhaye E., Jacquot JP., Didierjean C., Morel-Rouhier M. in vitro In vitro x-ray diffraction x-ray crystallography X-ray X-ray x-ray diffraction experimental particp experimental participant identification experimental particp Thuillier A., Roret T., Favier F., Gelhaye E., Jacquot JP., Didierjean C., Morel-Rouhier M. FEBS Lett. (0014-5793) 2013 Atypical features of a Ure2p glutathione transferase from Phanerochaete chrysosporium. Atypical features of a Ure2p glutathione transferase from Phanerochaete chrysosporium. FEBS Lett. (0014-5793) 2013 Thuillier A., Roret T., Favier F., Gelhaye E., Jacquot JP., Didierjean C., Morel-Rouhier M. in vitro In vitro enzymatic study enzymatic study predetermined predetermined participant predetermined Thuillier A., Roret T., Favier F., Gelhaye E., Jacquot JP., Didierjean C., Morel-Rouhier M. FEBS Lett. (0014-5793) 2013 i7a570_phach protein protein phach Phanerodontia chrysosporium White-rot fungus Sporotrichum pruinosum MATNTDKPVVHYTAPTPNGWVPAILLEELKAVYGGPDYETVKMSIRDADIGKVHNQVKSDWFLKICPNGRIPAITHEGFPVFETSAILLYLAQHFDKENAFSRDPVKDPKGYSEELQWLFFAHGGIGPMQGQANHFNLYAPEKIPYAINRYLNESKRLYRVLDDRLKGREYILGTYGIADIKIFGWARIAPRTGLDLDEFPNVKAWVERIEKRPAVQAGINSCN mint 41B2E71E7D123998 b3vqj6_phach GTO3 protein protein phach Phanerodontia chrysosporium White-rot fungus Sporotrichum pruinosum MPIPDEKIFPHATGAAAKTVEQHQDPQELVFYAGWFCPFVQRTWIALEERGIPYQYKEVNPYKKEKHFLDINPKGLVPAIEYKGKALYESIILCEFLEDAYPNYKPKLLPEDPFERAYARIWLDYISKSIIPANFRLIQAQTPEKQQEALADFNKALKQFAEKIKGPYFLGEQFSLVDIAIVPWIVRDYIIAENRGFKREDIGSKWVEYASKLEKRDSVARTSSEHYAEIYGRYLRDEAQSEAAKATRAGRDIP mint 38E8FA676A3BFAFA i7a570 1 PcUre2pB1 3 predetermined predetermined participant predetermined experimental particp experimental participant identification experimental particp unspecified role unspecified role neutral component neutral component purified purified Stoichiometry: 2.0 direct interaction direct interaction mint PDB ID: 4F0B f1 sf1 st2 gto3-i7a570 2 PcUre2pB1 3 predetermined predetermined participant predetermined experimental particp experimental participant identification experimental particp electron donor electron donor neutral component neutral component purified purified PcGTO3 4 predetermined predetermined participant predetermined experimental particp experimental participant identification experimental particp electron acceptor electron acceptor neutral component neutral component purified purified enzymatic reaction enzymatic reaction Biochemical reaction Biochemical reaction f4 mint PcUre2pB1 and PcUre2pB1N18A under their native or reduced form are not able to bind the probe (Fig. 4). Incubating PcGSTO3-SG with PcUre2pB1 previously reduced and dialyzed, revealed a fluorescent signal on SDS-PAGE gel. This suggests that PcGSTO3 has been reduced by PcUre2pB1 allowing the binding of the fluorescent probe onto the PcGSTO3 catalytic cysteine. The same experiment has been performed using heat inactivated reduced PcUre2pB1 to ensure that the detected activity is not due to residual DTT or GSH in the mixture. No signal was detected showing that the deglutathionylation activity of PcGSTO3 is indeed mediated by PcUre2pB1