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Kynureninase C-terminal domain
This entry represents de C-terminal domain of kynureninase [1-5], a member of a large family of catalytically diverse but structurally homologous pyridoxal 5'-phosphate (PLP) dependent enzymes. The Homo sapiens and other eukaryotic constitutive kynureninases preferentially catalyse the hydrolytic cleavage of 3-hydroxy-l-kynurenine to produce 3-hydroxyanthranilate and l-alanine, while l-kynurenine is the substrate of many prokaryotic inducible kynureninases [1-5].. Paper describing PDB structure 1qz9. [1]. 14756555. Three-dimensional structure of kynureninase from Pseudomonas fluorescens. Momany C, Levdikov V, Blagova L, Lima S, Phillips RS;. Biochemistry. 2004;43:1193-1203. Paper describing PDB structure 2hzp. [2]. 17300176. Crystal structure of Homo sapiens kynureninase. Lima S, Khristoforov R, Momany C, Phillips RS;. Biochemistry. 2007;46:2735-2744. Paper describing PDB structure 3e9k. [3]. 19143568. Crystal structure of the Homo sapiens kynureninase-3-hydroxyhippuric acid inhibitor complex: insights into the molecular basis of kynureninase substrate specificity. Lima S, Kumar S, Gawandi V, Momany C, Phillips RS;. J Med Chem. 2009;52:389-396. Paper describing PDB structure 4pjq. [4]. 25517350. An artificial PPR scaffold for programmable RNA recognition. Coquille S, Filipovska A, Chia T, Rajappa L, Lingford JP, Razif MF, Thore S, Rackham O;. Nat Commun. 2014;5:5729. Paper describing PDB structure 5i90. [5]. 27139833. 1.2 A resolution crystal structure of the periplasmic aminotransferase PvdN from Pseudomonas aeruginosa. Drake EJ, Gulick AM;. Acta Crystallogr F Struct Biol Commun. 2016;72:403-408. (from Pfam)
aminotransferase class V-fold PLP-dependent enzyme
This domain is found in amino transferases, and other enzymes including cysteine desulphurase EC:4.4.1.-. (from Pfam)
kynureninase
This HMM describes kynureninase, a pyridoxal-phosphate enzyme. Kynurinine is a Trp breakdown product and a precursor for NAD. In Chlamydia psittaci, an obligate intracellular pathogen, kynureninase makes anthranilate, a Trp precursor, from kynurenine. This counters the tryptophan hydrolysis that occurs in the host cell in response to the pathogen.
kynureninase is a pyridoxal-5'-phosphate (PLP)-dependent enzyme, which catalyses the cleavage of kynurenine (Kyn) into anthranilic acid (Ant)
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