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2.6.1.113 |
Description |
Putrescine--pyruvate transaminase |
Alternative names |
Putrescine--pyruvate transaminase;
PATase;
SpuC (gene name) |
Catalyzed reaction |
putrescine + pyruvate = 4-aminobutanal + L-alanine. |
Cofactor |
Pyridoxal phosphate. |
Comments |
The enzyme, studied in the bacterium Pseudomonas aeruginosa, participates in a putrescine degradation pathway. |
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Distinct from 2.6.1.82 because the preferred ketoacid substrate is pyruvate rather than 2-oxoglutarate. As with 2.6.1.82, the 4-aminobutanal undergoes spontaneous cyclization, forming 1-pyrroline.
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PDB |
6HX9; |
Organisms |
-Eubacteria |
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Family |
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Links |
Enzyme (activities) 2.6.1.113
BRENDA (activities) 2.6.1.113
KEGG (pathways) 2.6.1.113
PLPMDB (PLP mutants) 2.6.1.113
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References |
Galman JL, Gahloth D, Parmeggiani F, Slabu I, Leys D, Turner NJ (2018) Characterization of a Putrescine Transaminase From Pseudomonas putida and its Application to the Synthesis of Benzylamine Derivatives Front Bioeng Biotechnol 6 205. Galman,J.L., Slabu,I., Weise,N.J., Iglesias,C., Parmeggiani,F., Lloyd,R.C. and Turner,N.J. (2017) Biocatalytic transamination with near-stoichiometric inexpensive amine donors mediated by bifunctional mono- and di-amine transaminases Green Chem 19 361-366. Wilding M, Walsh EF, Dorrian SJ, Scott C (2015) Identification of novel transaminases from a 12-aminododecanoic acid-metabolizing Pseudomonas strain Microb Biotechnol 8 665-72. Lu CD, Itoh Y, Nakada Y, Jiang Y. (2002) Functional analysis and regulation of the divergent spuABCDEFGH-spuI operons for polyamine uptake and utilization in Pseudomonas aeruginosa PAO1 J Bacteriol 184 3765-73. Articles on 2.6.1.113 |
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last changed |
2019/01/14 13:32 |
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