Abstract
The putrescine aminotransferase KES24511 from Pseudomonas sp. strain AAC was previously identified as an industrially relevant enzyme based on the discovery that it is able to promiscuously catalyse the transamination of 12-aminododecanoic acid. Here, the cloning, heterologous expression, purification and successful crystallization of the KES24511 protein are reported, which ultimately generated crystals adopting space group I2. The crystals diffracted X-rays to 2.07 Å resolution and data were collected using the microfocus beamline of the Australian Synchrotron. The structure was solved using molecular replacement, with a monomer from PDB entry 4a6t as the search model.
Keywords:
12-aminododecanoic acid; PLP-dependent; aminotransferases; transaminase.
MeSH terms
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Amino Acid Sequence
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Bacterial Proteins / chemistry*
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Bacterial Proteins / genetics
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Bacterial Proteins / metabolism
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Binding Sites
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Cloning, Molecular
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Crystallography, X-Ray
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Escherichia coli / genetics
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Escherichia coli / metabolism
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Gene Expression
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Lauric Acids / chemistry*
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Lauric Acids / metabolism
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Models, Molecular
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Plasmids / chemistry
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Plasmids / metabolism
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Protein Binding
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Protein Conformation, alpha-Helical
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Protein Conformation, beta-Strand
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Protein Interaction Domains and Motifs
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Protein Multimerization
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Pseudomonas / chemistry*
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Pseudomonas / enzymology
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Recombinant Proteins / chemistry
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Recombinant Proteins / genetics
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Recombinant Proteins / metabolism
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Substrate Specificity
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Transaminases / chemistry*
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Transaminases / genetics
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Transaminases / metabolism
Substances
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Bacterial Proteins
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Lauric Acids
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Recombinant Proteins
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12-aminododecanoic acid
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Transaminases
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diamine aminotransferase