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Prokaryotic homologs of the eukaryotic 3-hydroxyanthranilate 3,4-dioxygenase and 2-amino-3-carboxymuconate-6-semialdehyde decarboxylase in the 2-nitrobenzoate degradation pathway of Pseudomonas fluorescens strain KU-7.
Muraki T, Taki M, Hasegawa Y, Iwaki H, Lau PC. Muraki T, et al. Among authors: hasegawa y. Appl Environ Microbiol. 2003 Mar;69(3):1564-72. doi: 10.1128/AEM.69.3.1564-1572.2003. Appl Environ Microbiol. 2003. PMID: 12620844 Free PMC article.
Alpha-amino-beta-carboxymuconic-epsilon-semialdehyde decarboxylase (ACMSD) is a new member of the amidohydrolase superfamily.
Li T, Iwaki H, Fu R, Hasegawa Y, Zhang H, Liu A. Li T, et al. Among authors: hasegawa y. Biochemistry. 2006 May 30;45(21):6628-34. doi: 10.1021/bi060108c. Biochemistry. 2006. PMID: 16716073
The enzymatic activity of Pseudomonas fluorescens alpha-amino-beta-carboxymuconic-epsilon-semialdehyde decarboxylase (ACMSD) is critically dependent on a transition metal ion [Li, T., Walker, A. L., Iwaki, H., Hasegawa, Y., and Liu, A. (2005) J. Am. Chem. Soc. 127, …
The enzymatic activity of Pseudomonas fluorescens alpha-amino-beta-carboxymuconic-epsilon-semialdehyde decarboxylase (ACMSD) is critically d …
4,677 results