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Image Search Results
Journal: The Plant Cell
Article Title: From Amino Acid to Glucosinolate Biosynthesis: Protein Sequence Changes in the Evolution of Methylthioalkylmalate Synthase in Arabidopsis
doi: 10.1105/tpc.110.079269
Figure Lengend Snippet: Sequences of Two Regions in the IPMS/MAM Protein Family (Prosite Motifs PS00815 and PS00816) That Are Responsible for Divalent Metal Cofactor Binding in Mt-IPMS
Article Snippet: In contrast with microbial IPMSs and the MAMs, plant IPMSs have the second His replaced by a Gln in the HxH[DN]D sequence. table ft1 table-wrap mode="anchored" t5 Table 1. caption a7 Enzyme a PS00815 LR[ DE ]GxQxxxx{L}xxxxxK b PS00816 [LIVMF]xx H x H [DN]D xGx[GAS]x[GASLI] b IPMS1/IPMS2 Arabidopsis LR D GeQspgaTltskeK Ist H c Q ND lGlStA IPMSa/IPMSb Solanum pennellii LR D GeQspgaTmttkeK Ist H c Q ND lGlStA IPMSa/IPMSb Oryza sativa LR D GeQspgaTltsaeK Ist H c Q ND lGlAtA IPMS
Techniques: Binding Assay
Journal: The Plant Cell
Article Title: From Amino Acid to Glucosinolate Biosynthesis: Protein Sequence Changes in the Evolution of Methylthioalkylmalate Synthase in Arabidopsis
doi: 10.1105/tpc.110.079269
Figure Lengend Snippet: Dimer Structure of M. tuberculosis IPMS (Koon et al., 2004) Deposited in the Protein Data Bank (1SR9) and Drawn with PYMOL.
Article Snippet: Structural data for
Techniques:
Journal: The Plant Cell
Article Title: From Amino Acid to Glucosinolate Biosynthesis: Protein Sequence Changes in the Evolution of Methylthioalkylmalate Synthase in Arabidopsis
doi: 10.1105/tpc.110.079269
Figure Lengend Snippet: Alignment of Deduced Amino Acid Sequences for the IPMS and MAM Enzymes of Arabidopsis and the IPMS of M. tuberculosis (PDB 1SR9).
Article Snippet: Structural data for
Techniques: