Archives of biochemistry and biophysics, 317(1), 93-102 (1995-02-20)
Peptidylglycine alpha-amidating enzyme catalyzes the two-step conversion of C-terminal glycine-extended peptides to C-terminal alpha-amidated peptides and glyoxylate in a reaction that requires O2, ascorbate and 2 mol of copper per mole of enzyme [Kulathila et al. (1994) Arch. Biochem. Biophys.
European journal of biochemistry, 267(11), 3264-3269 (2000-05-29)
The presteady-state and steady-state kinetics of bovine serum amine oxidase (BSAO) were analyzed by stopped-flow transient spectroscopy. A simplified model of the catalytic cycle was found to describe the experimental data and the rate constants of the individual steps were
The Biochemical journal, 260(1), 19-25 (1989-05-15)
Bovine serum amine oxidase is inhibited by benzylhydrazine (BHy), but recovers full activity after a few hours incubation [Hucko-Haas & Reed (1970) Biochem. Biophys. Res. Commun. 38, 396-400]. The first phase of the process, requiring about 15 min, was found
A series of indole-2-carboxylic acid benzylidene-hydrazides has been identified as a new class of potent apoptosis inducers through a novel cell-based caspase HTS assay. The screening hit, 5-chloro-3-methyl-indole-2-carboxylic acid (4-nitrobenzylidene)-hydrazide (3a), was found to arrest T47D cells in G(2)/M and
Peptidylglycine alpha-hydroxylating monooxygenase (PHM; EC 1.14.17.3) catalyses the rate-limiting step in the post-translational activation of substance P, among other neuropeptides, from its glycine-extended precursor. Comparative kinetic studies were performed, using trans-styrylacetic acid or trans-styrylthioacetic acid as known mechanism-based inhibitors, of
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