Kynureninase-Type enzymes of Penicillum roqueforti, Aspergillus niger, Rhizopus stolonifer, and Pseudomonas fluorescens: further evidence for distinct kynureninase and hydroxykynureninase activities
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منابع مشابه
Kynureninase-Type enzymes of Penicillum roqueforti, Aspergillus niger, Rhizopus stolonifer, and Pseudomonas fluorescens: further evidence for distinct kynureninase and hydroxykynureninase activities.
The kynureninase-type enzymes of three fungi and one bacterium were isolated and examined kinetically for their ability to catalyze the hydrolysis of L-kynurenine and L-3-hydroxykynurenine. The phycomycete Rhizopus stolonifer was found to contain a single, constitutive enzyme with Km for L-3-hydroxykynurenine and L-kynurenine of 6.67 times 10-minus 6 and 2.5 times 10-minus 4 M, respectively. Th...
متن کاملThe kynureninase of Pseudomonas fluorescens.
Kotake and Nakayama (1) observed the conversion of kynurenine to anthranilic acid and alanine by a mammalian liver extract. Subsequently the enzyme responsible for this reaction in the mammal was partly purified (2,3) and the enzyme, prepared from vitamin Be-deficient animals, was shown to require pyridoxal phosphate for its maximal activity (2). During an investigation of tryptophan metabolism...
متن کاملFurther Purification and Some Properties of Kynureninase.
The enzyme kynureninase converts kynurenine and hydroxykynurenine to alanine and anthranilic acid and to alanine and hydroxyanthranilic acid, respectively14>. Previously, Knox 51, Jakoby et al. 4>, a~d Wiss et al. 6> have described the purification and some properties of kynureninase. According to their reports, this enzyme obtained from bacteria was activated with magnesium ions, while it from...
متن کاملKynureninase from Neurospora: Purification
As part of a study of kynurenine metabolism in Neurospora crassa, the enzyme, kynureninase, has been investigated. Evidence from studies with mycelial pads suggests that tryptophan gives rise to kynurenine, which may be degraded to anthranilic acid (1). Kynurenine is also oxidized to hydroxykynurenine, which is converted to hydroxyanthranilic acid (2). The similarity of these reactions, i.e. th...
متن کاملProperties and partial purification of kynureninase.
involvement with the carbohydrate moiety (cf. Porter, 1950). Although the acid lability of certain c-DNP-amino acids cannot be ignored (e.g. proline, Porter & Sanger, 1948), no evidence has been obtained for the presence of even traces of ca-DNPamino acids. Bailey (1951) could find only a trace of oc-DNP-residue (1 mole/106 g. of protein) in four-times-recrystallized ovalbumin. The availability...
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ژورنال
عنوان ژورنال: Journal of Bacteriology
سال: 1975
ISSN: 0021-9193,1098-5530
DOI: 10.1128/jb.122.1.235-244.1975