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Equilibria and absorption spectra of tryptophanase.
Refinement and Comparisons of the Crystal Structures of Pig Cytosolic Aspartate Aminotransferase and Its Complex with 2-Methylaspartate*
A stereochemical mechanism for the open-to-closed transition that involves the electrostatic neutralization of two active site arginine residues by the negative charges of the incoming substrate, a large change in the backbone (φ,ψ) conformational angles of two key glycine residues, and the entropy-driven burial of a stretch of hydrophobic residues on the N-terminal helix is proposed.
Equilibriums and absorption spectra of Schiff bases
Quantitative description of absorption spectra of a pyridoxal phosphate-dependent enzyme using lognormal distribution curves.
The Widespread Applicability of Lognormal Curves for the Description of Absorption Spectra
We have fitted over 160 electronic absorption spectra of over 95 aromatic compounds and some other substances with lognormal distribution curves to evaluate the shapes of the bands. The compounds…
Spectroscopic studies of quinonoid species from pyridoxal 5'-phosphate.
The analysis establishes that in all species a proton remains on either the phenolic oxygen or the imine nitrogen, and suggests that the latter may, in fact, be a quinonoid form, either alone or in rapid equilibrium with the Schiff base.
NMR spectra of exchangeable protons of pyridoxal phosphate-dependent enzymes.
Crystalline enzyme.substrate complexes of asparate aminotransferase.
- C. M. Metzler, D. Metzler, D. Martin, R. Newman, A. Arnone, P. Rogers
- ChemistryThe Journal of biological chemistry
- 10 August 1978
X-ray diffraction studies show that the crystals with erythro-beta-hydroxy aspartate and alpha-methylaspartate are isomorphous with those of both alpha and beta subforms of the native enzyme.
Correlation of polarized absorption spectroscopic and X-ray diffraction studies of crystalline cytosolic aspartate aminotransferase of pig hearts.