Nothing Special   »   [go: up one dir, main page]

Fitzpatrick et al., 1982 - Google Patents

The kinetic mechanism of D-amino acid oxidase with D-alpha-aminobutyrate as substrate. Effect of enzyme concentration on the kinetics.

Fitzpatrick et al., 1982

View PDF
Document ID
9687048186050556547
Author
Fitzpatrick P
Massey V
Publication year
Publication venue
Journal of Biological Chemistry

External Links

Snippet

The kinetic mechanism of hog kidney D-amino acid oxidase with D-alpha-aminobutyrate as substrate has been examined in detail using a combination of steady state and rapid reaction methods. At concentrations of D-alpha-aminobutyrate below 0.5 mM, the rapid …
Continue reading at www.sciencedirect.com (PDF) (other versions)

Similar Documents

Publication Publication Date Title
Wariishi et al. Manganese peroxidase from the lignin-degrading basidiomycete Phanerochaete chrysosporium: transient state kinetics and reaction mechanism
Alberty Enzyme kinetics
Bull et al. Kinetic studies of superoxide dismutases: properties of the manganese-containing protein from Thermus thermophilus
Fitzpatrick et al. The kinetic mechanism of D-amino acid oxidase with D-alpha-aminobutyrate as substrate. Effect of enzyme concentration on the kinetics.
Coles et al. Inactivation of succinate dehydrogenase by 3-nitropropionate.
Bright et al. 7 flavoprotein oxidases
Jourd’heuil et al. Dynamic state of S-nitrosothiols in human plasma and whole blood
Husain et al. Kinetic studies on the reaction of p-hydroxybenzoate hydroxylase. Agreement of steady state and rapid reaction data.
Critchlow et al. Studies on horseradish peroxidase: X. The mechanism of the oxidation of p-cresol, ferrocyanide, and iodide by compound II
Arciero et al. Spectroscopic and rapid kinetic studies of reduction of cytochrome c554 by hydroxylamine oxidoreductase from Nitrosomonas europaea
Nishino et al. The reactivity of chicken liver xanthine dehydrogenase with molecular oxygen
Jones et al. On the mechanism of compound I formation from peroxidases and catalases
JPS603835B2 (en) Trinder reagent and method for analyzing hydrogen peroxide using it
Palfey et al. Changes in the catalytic properties of p-hydroxybenzoate hydroxylase caused by the mutation Asn300Asp
Michuda et al. Distinctions in the equilibrium kinetic constants of the mitochondrial and supernatant isozymes of aspartate transaminase
JPS59132900A (en) Test system and method for measuring nad(p)h
Portsmouth et al. The peroxidase activity of deuterohemin
Carrico et al. A Study of the Reduction and Oxidation of Human Ceruloplasmin: Evidence that a Diamagnetic Chromophore in the Enzyme Participates in the Oxidase Mechanism
Holzhütter et al. A kinetic model for the interaction of nitric oxide with a mammalian lipoxygenase
Ljones Nitrogenase from Clostridium pasteurianum. Changes in optical absorption spectra during electron transfer and effects of ATP, inhibitors and alternative substrates
Kuntzleman et al. Reduction-induced inhibition and Mn (II) release from the photosystem II oxygen-evolving complex by hydroquinone or NH2OH are consistent with a Mn (III)/Mn (III)/Mn (IV)/Mn (IV) oxidation state for the dark-adapted enzyme
Kuznetsova et al. Reactions of spinach nitrite reductase with its substrate, nitrite, and a putative intermediate, hydroxylamine
Kwan et al. Spectral properties of Co (II)-and Ni (II)-activated rabbit muscle pyruvate kinase.
Boettcher et al. Itemizing enzyme ligand interactions in native and half-active hybrid aspartate transaminase to probe site-site relations
Tegoni et al. Resonance Raman study on the oxidized and anionic semiquinone forms of flavocytochrome b 2 and L-lactate monooxygenase. Influence of the structure and environment of the isoalloxazine ring on the flavin function