3.7.1.3: kynureninase
This is an abbreviated version!
For detailed information about kynureninase, go to the full flat file.
Word Map on EC 3.7.1.3
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3.7.1.3
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3-hydroxyanthranilic
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medicine
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quinolinic
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3-hydroxykynurenine
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kynurenic
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anthranilic
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indoleamine
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3-monooxygenase
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l-tryptophan
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ido
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3,4-dioxygenase
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xanthurenic
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aminocarboxymuconate-semialdehyde
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3-hydroxylase
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quin
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excitotoxins
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quinonoid
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pyrrolase
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marginalis
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indoleamine-2,3-dioxygenase
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synthesis
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b6-deficient
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drug development
- 3.7.1.3
-
3-hydroxyanthranilic
- medicine
-
quinolinic
- 3-hydroxykynurenine
-
kynurenic
-
anthranilic
- indoleamine
-
3-monooxygenase
- l-tryptophan
-
ido
-
3,4-dioxygenase
-
xanthurenic
- aminocarboxymuconate-semialdehyde
-
3-hydroxylase
-
quin
-
excitotoxins
-
quinonoid
-
pyrrolase
- marginalis
- indoleamine-2,3-dioxygenase
- synthesis
-
b6-deficient
- drug development
Reaction
Synonyms
HsKynase, Kynase, KYNU, kynureninase, L-kynurenine hydrolase, PfKynase
ECTree
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Crystallization
Crystallization on EC 3.7.1.3 - kynureninase
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crystals of recombinant kynureninase that diffracted to 2.0 A are obtained, and the atomic structure of the PLP-bound holoenzyme is determined by molecular replacement using the Pseudomonas fluorescens structure as the phasing model
the wild type enzyme is cocrystallized with 3-hydroxyhippuric acid, using the modified microbatch under oil technique at 25?C, with 0.05 M MgCl2, 0.1 M Tris (pH 8.0), and 25% (w/v) PEG 3000
by hanging-drop vapor diffusion method at room temperature, to 1.85 A resolution, Lys-227 is the pyridoxal-5'-phosphate binding residue near the pyridoxal-5'-phosphate nitrogen, but Asp-132 is also strictly conserved and at a similar distance from the pyridinium nitrogen, Tyr-226 donates a hydrogen bond to the phosphate of pyridoxal-5'-phosphate, Trp-256 donates a hydrogen bond to the phosphate through the indole N1-hydrogen