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苯丙氨酸托氢镁

苯丙氨酸托氢镁结构式
苯丙氨酸托氢镁结构式
品牌特惠专场
常用名 苯丙氨酸托氢镁 英文名 l-phenylalanine dehydrogenase
CAS号 69403-12-9 分子量 412.386
密度 1.3±0.1 g/cm3 沸点 505.8±50.0 °C at 760 mmHg
分子式 C22H18F2N2O4 熔点 N/A
MSDS 美版 闪点 259.7±30.1 °C

Fundamental differences in bioaffinity of amino acid dehydrogenases for N6- and S6-linked immobilized cofactors using kinetic-based enzyme-capture strategies.

Anal. Biochem. 338(1) , 102-12, (2005)

Five different immobilized NAD+ derivatives were employed to compare the behavior of four amino acid dehydrogenases chromatographed using kinetic-based enzyme capture strategies (KBECS): S6-, N6-, N1-, 8'-azo-, and pyrophosphate-linked immobilized NAD+. The a...

Cloning, sequencing, and expression of Rhodococcus L-phenylalanine dehydrogenase. Sequence comparisons to amino-acid dehydrogenases.

J. Biol. Chem. 269 , 16203-16211, (1994)

L-Phenylalanine dehydrogenase catalyzes the NAD(+)-dependent, reversible, oxidative deamination of L-phenylalanine to form ammonia, phenyl pyruvate, and NADH. The enzyme has been purified to homogeneity from Rhodococcus sp. M4, and a partial amino acid sequen...

Phenylalanine dehydrogenase of Bacillus badius. Purification, characterization and gene cloning.

Eur. J. Biochem. 168(1) , 153-9, (1987)

Phenylalanine dehydrogenase produced by Bacillus badius IAM 11059 was purified from the crude extract of B. badius to homogeneity, as judged by disc gel electrophoresis. The enzyme has an isoelectric point of 3.5 and a relative molecular mass, Mr, of 310,000-...

Novel phenylalanine dehydrogenases from Sporosarcina ureae and Bacillus sphaericus. Purification and characterization.

J. Biol. Chem. 262(21) , 10346-54, (1987)

NAD+-dependent phenylalanine dehydrogenases were purified 1,500- and 1,600-fold, and crystallized from Sporosarcina ureae SCRC-R04 and Bacillus sphaericus SCRC-R79a, respectively. The purified enzymes were homogeneous as judged by disc gel electrophoresis. Th...

Enzymatic phenylalanine estimation for the management of patients with phenylketonuria.

Clin. Chim. Acta 201(1-2) , 95-8, (1991)

Crystallization of NAD+-dependent phenylalanine dehydrogenase from Nocardia sp239.

Acta Crystallogr. D Biol. Crystallogr. 54(Pt 2) , 269-72, (1998)

The NAD+-dependent phenylalanine dehydrogenase from Nocardia sp239 has been crystallized by the hanging-drop method of vapour diffusion using ammonium sulfate as the precipitant. Two crystal forms were obtained in the presence and absence of the enzyme substr...

Rhodococcus L-phenylalanine dehydrogenase: kinetics, mechanism, and structural basis for catalytic specificity.

Biochemistry 39(31) , 9174-87, (2000)

Phenylalanine dehydrogenase catalyzes the reversible, pyridine nucleotide-dependent oxidative deamination of L-phenylalanine to form phenylpyruvate and ammonia. We have characterized the steady-state kinetic behavior of the enzyme from Rhodococcus sp. M4 and ...

Synthesis of a highly substituted N(6)-linked immobilized NAD(+) derivative using a rapid solid-phase modular approach: suitability for use with the kinetic locking-on tactic for bioaffinity purification of NAD(+)-dependent dehydrogenases.

Protein Expr. Purif. 20(3) , 421-34, (2000)

This study is concerned with further development of the kinetic locking-on strategy for bioaffinity purification of NAD(+)-dependent dehydrogenases. Specifically, the synthesis of highly substituted N(6)-linked immobilized NAD(+) derivatives is described usin...