Phenylalanine Hydroxylase from Pseudomonas Species (ATCC 11299a)

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Biosynthesis of pteridines and of phenylalanine hydroxylase cofactor in cell-free extracts of Pseudomonas species (ATCC 11299a).

A cell-free system for the synthesis of a phenylalanine hydroxylase cofactor from guanosine triphosphate was obtained from extracts of Pseudomonas species (ATCC 11299a). This preparation produced formic acid from the ureido carbon of labeled GTP. The preparation also made specific pteridines from GTP. Among the products, xanthopterin, neopterin, and a cyclic phosphate derivative of neopterin we...

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Mouse phenylalanine hydroxylase. Homology and divergence from human phenylalanine hydroxylase.

The laboratory mouse represents an important model for the study of phenylalanine metabolism and the pathochemistry of phenylketonuria, yet mouse phenylalanine hydroxylase (PAH) has not been extensively studied. We report the cloning and sequencing of a mouse PAH cDNA, the expression of enzymic activity from the mouse PAH cDNA clone and the identification of mouse PAH and human PAH by two-dimen...

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Enzymatic Formation of Phenylpyruvic Acid in Pseudomonas Sp. (atcc 11299a) and Its Regulation.

The early steps in the biosynthesis of the aromatic amino acids in microorganisms leading to the formation of alicyclic precursors are rather well known (1, 2). Information regarding the regulation of these steps is beginning to accumulate (3, 4). A considerable gap, however, still exists in our knowledge about the properties and the regulation of the enzymes involved in the final aromatization...

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Characterization of phenylalanine hydroxylase.

Iron can be bound to phenylalanine hydroxylase (PAH) in two environments. The assignment of the electron paramagnetic resonance spectrum of PAH to two, overlapping high-spin ferric signals is confirmed by computer simulation. Both environments are shown to be populated in the crude enzyme. Reconstitution of the apoenzyme demonstrated that the two iron environments are not interconvertible. Oxyg...

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ژورنال

عنوان ژورنال: Journal of Biological Chemistry

سال: 1967

ISSN: 0021-9258

DOI: 10.1016/s0021-9258(18)95857-6