Sandbox Reserved 1665: Difference between revisions
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Mutation in the octanal binding site did occur and made certain changes as well. Asn 159, Trp 160, Ser 292, Leu 419, Phe 456 were the amino acids residues that got most disrupted. The reason behind this was that these amino acid residues were closer to the catalytic site of AldC than those other residues who receive a lesser disruption from the activity. From the table we can see as well N159 and L419 mutants lacked significant activity. | Mutation in the octanal binding site did occur and made certain changes as well. Asn 159, Trp 160, Ser 292, Leu 419, Phe 456 were the amino acids residues that got most disrupted. The reason behind this was that these amino acid residues were closer to the catalytic site of AldC than those other residues who receive a lesser disruption from the activity. From the table we can see as well N159 and L419 mutants lacked significant activity. | ||
== Structural highlights == | == Structural highlights ==Secondary structure has feature and domains, the N-terminus of the protein contains a central Beta sheet that is surrounded by alpha helices to form the NAD(H)-binding site. Around the C-Terminus end of the protein it consists a mix of alpha/beta domains, which include a catalytic cysteine residue and forms the aldehyde -binding site. The article mentions as well what connects the N and C terminal domains of the protein AldC is by an interdomain linker region. | ||
