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 http://mint.bio.uniroma2.it/mint budiman-2009-1 Engineering of monomeric FK506-binding protein 22 with peptidyl prolyl cis-trans isomerase. Importance of a V-shaped dimeric structure for binding to protein substrate. in vitro In vitro spr surface plasmon resonance Optical biosensor BIAcore(r) BIAcore(r) Optical biosensor spr predetermined predetermined participant predetermined Budiman C., Bando K., Angkawidjaja C., Koga Y., Takano K., Kanaya S. FEBS J. (1742-464X) 2009 lalba_bovin Alpha-lactalbumin LALBA ALACTA Lactose synthase B protein protein protein bovin Bos taurus (Bovine) Bovine MMSFVSLLLVGILFHATQAEQLTKCEVFRELKDLKGYGGVSLPEWVCTTFHTSGYDTQAIVQNNDSTEYGLFQINNKIWCKDDQNPHSSNICNISCDKFLDDDLTDDIMCVKKILDKVGINYWLAHKALCSEKLDQWLCEKL mint homomint Regulatory subunit of lactose synthase, changes the substrate specificity of galactosyltransferase in the mammary gland making glucose a good acceptor substrate for this enzyme. This enables LS to synthesize lactose, the major carbohydrate component of milk. In other tissues, galactosyltransferase transfers galactose onto the N-acetylglucosamine of the oligosaccharide chains in glycoproteins q765b0_9gamm Peptidyl-prolyl cis-trans isomerase fklB protein protein shewanella sp. sib1 Shewanella sp. SIB1 MSDLFSTMEQHASYGVGRQMGEQLAANSFEGIDIPAVQAGLADAFAGKESAVSMEELQVAFTEISRRLQAAQEAAAEAAAAEGDTFLAENAKRDGITITESGLQYEVLVQGDGETPTYDSTVRTHYHGTFISGDVFDSSVARGQPAEFPVSGVIAGWTEALQLMPVGTKLKLYVPHHLAYGERGAGASIPPYSALVFEVELLEII mint fklb-lalba 821947 lalba_bovin Alpha-lactalbumin 821948 predetermined predetermined participant predetermined unspecified role unspecified role prey prey purified purified q765b0_9gamm FKBP22 821949 predetermined predetermined participant predetermined unspecified role unspecified role bait bait purified purified direct interaction direct interaction false false false 821947 F5 mint Kd value for binding of reduced α-lactalbumin to NNC-FKBP22 was determined to be 42.5±2.1 μM.