IntAct European Bioinformatics Institute IntAct intact http://www.ebi.ac.uk/ http://www.ebi.ac.uk/intact/query/${ac} EBI-[0-9]+|IA:[0-9]+ INTerAction database (IntAct) provides an open source database and toolkit for the storage, presentation and analysis of molecular interactions. http://www.ebi.ac.uk/intact European Bioinformatics Institute; Wellcome Trust Genome Campus; Hinxton, Cambridge; CB10 1SD; United Kingdom http://www.ebi.ac.uk/intact/ Mutations in the regulatory subunit of yeast acetohydroxyacid synthase affect its activation by MgATP. Mutations in the regulatory subunit of yeast acetohydroxyacid synthase affect its activation by MgATP. Biochem. J. (0264-6021) 2006 imex curation Lee Y.T., Duggleby R.G. ronald.duggleby@uq.edu.au 11-Jun-2014: Contacted by IntAct-Help. Only protein-protein interactions in vitro In vitro enzymatic study enzymatic study predetermined predetermined participant predetermined Lee Y.T., Duggleby R.G. Catalysis of pyruvate to 2-acetolactate by the reconstituted acetolactate synthase was monitored using a colorimetric assay. ronald.duggleby@uq.edu.au Accepted 2014-MAY-16 by MGT Biochem. J. (0264-6021) 2006 Only protein-protein interactions imex curation pyruvate pyruvate small molecule small molecule chemical synthesis Chemical synthesis (Chemical synthesis) ilvb_yeast Acetolactate synthase catalytic subunit, mitochondrial ILV2 SMR1 YMR108W YM9718.07 Acetohydroxy-acid synthase catalytic subunit protein protein yeast Saccharomyces cerevisiae Baker's yeast MIRQSTLKNFAIKRCFQHIAYRNTPAMRSVALAQRFYSSSSRYYSASPLPASKRPEPAPSFNVDPLEQPAEPSKLAKKLRAEPDMDTSFVGLTGGQIFNEMMSRQNVDTVFGYPGGAILPVYDAIHNSDKFNFVLPKHEQGAGHMAEGYARASGKPGVVLVTSGPGATNVVTPMADAFADGIPMVVFTGQVPTSAIGTDAFQEADVVGISRSCTKWNVMVKSVEELPLRINEAFEIATSGRPGPVLVDLPKDVTAAILRNPIPTKTTLPSNALNQLTSRAQDEFVMQSINKAADLINLAKKPVLYVGAGILNHADGPRLLKELSDRAQIPVTTTLQGLGSFDQEDPKSLDMLGMHGCATANLAVQNADLIIAVGARFDDRVTGNISKFAPEARRAAAEGRGGIIHFEVSPKNINKVVQTQIAVEGDATTNLGKMMSKIFPVKERSEWFAQINKWKKEYPYAYMEETPGSKIKPQTVIKKLSKVANDTGRHVIVTTGVGQHQMWAAQHWTWRNPHTFITSGGLGTMGYGLPAAIGAQVAKPESLVIDIDGDASFNMTLTELSSAVQAGTPVKILILNNEEQGMVTQWQSLFYEHRYSHTHQLNPDFIKLAEAMGLKGLRVKKQEELDAKLKEFVSTKGPVLLEVEVDKKVPVLPMVAGGSGLDEFINFDPEVERQQTELRHKRTGGKH B03C4D0F38AA1362 B03C4D0F38AA1362 ilv6_yeast Acetolactate synthase small subunit, mitochondrial ILV6 YCL009C YCL9C Acetohydroxy-acid synthase small subunit protein protein yeast Saccharomyces cerevisiae Baker's yeast MLRSLLQSGHRRVVASSCATMVRCSSSSTSALAYKQMHRHATRPPLPTLDTPSWNANSAVSSIIYETPAPSRQPRKQHVLNCLVQNEPGVLSRVSGTLAARGFNIDSLVVCNTEVKDLSRMTIVLQGQDGVVEQARRQIEDLVPVYAVLDYTNSEIIKRELVMARISLLGTEYFEDLLLHHHTSTNAGAADSQELVAEIREKQFHPANLPASEVLRLKHEHLNDITNLTNNFGGRVVDISETSCIVELSAKPTRISAFLKLVEPFGVLECARSGMMALPRTPLKTSTEEAADEDEKISEIVDISQLPPG BF36073D89BC0065 ilv2-ilv6 1 4 ancillary ancillary unspecified role unspecified role n-terminal his tag his tag Hexa-His-tag 6-His-tag Histidine-tag Hexa-His-tag Histidine-tag 6-His-tag n-term range n-terminal range n-term range n-term range n-terminal range n-term range P25605:p.Lys218Ala mutation decreasing rate mutation decreasing interaction rate mutation decreasing rate certain certain sequence position certain certain certain sequence position certain K A Wed May 02 15:17:50 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'lys218ala' Tue Jun 30 17:39:51 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Lys218Ala' P25605:p.His219Ala mutation decreasing rate mutation decreasing interaction rate mutation decreasing rate certain certain sequence position certain certain certain sequence position certain H A Wed May 02 17:04:02 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'his219ala' Tue Jun 30 18:05:27 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.His219Ala' region sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain P25605:p.Arg216Ala mutation decreasing rate mutation decreasing interaction rate mutation decreasing rate certain certain sequence position certain certain certain sequence position certain R A Wed May 02 15:01:58 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'arg216ala' Tue Jun 30 20:05:08 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Arg216Ala' P25605:p.His205Ala mutation decreasing rate mutation decreasing interaction rate mutation decreasing rate certain certain sequence position certain certain certain sequence position certain H A Wed May 02 19:09:35 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'his205ala' Tue Jun 30 18:40:20 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.His205Ala' ecoli Escherichia coli (strain K12) 3 enzyme enzyme unspecified role unspecified role n_terminus his tag his tag Hexa-His-tag 6-His-tag Histidine-tag Hexa-His-tag Histidine-tag 6-His-tag n-term range n-terminal range n-term range n-term range n-terminal range n-term range region sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain ecoli Escherichia coli (strain K12) 2 enzyme target enzyme target substrate substrate unspecified role unspecified role 10 15 enzymatic reaction enzymatic reaction Biochemical reaction Biochemical reaction His205Ala, Arg216ala, Lys218Ala, His219Ala and Leu222Ala abolish MgATP activation of the enzyme and probably constitute the binding site for this regulatory ligand.Ilv6 mutated at Leu177Aala, Phe204Ala, Pro206Ala and Ser212Ala only weakly stimulate the catalystic subunit but each of them is strongly activated by MgATP. The resulting enzyme is then inhibited by valine. Figs. 2-4, Table 2