Spinach chloroplast 0-acetylserine (thiol)-lyase exhibits two catalytically non-equivalent pyridoxal-5'-phosphate-containing active sites.
Rolland, N
Spinach chloroplast 0-acetylserine (thiol)-lyase exhibits two catalytically non-equivalent pyridoxal-5'-phosphate-containing active sites. [electronic resource] - European journal of biochemistry Feb 1996 - 272-82 p. digital
Publication Type: Journal Article; Research Support, Non-U.S. Gov't
0014-2956
10.1111/j.1432-1033.1996.00272.x doi
Amino Acid Sequence
Base Sequence
Binding Sites
Carbon-Oxygen Lyases
Catalysis
Chloroplasts--enzymology
Cysteine Synthase--chemistry
Escherichia coli--genetics
Fluorescent Dyes
Fluorometry
Genes, Plant
Genes, Synthetic
Kinetics
Lyases--chemistry
Models, Chemical
Molecular Sequence Data
Multienzyme Complexes
Protein Conformation
Pyridoxal Phosphate--chemistry
Recombinant Proteins--chemistry
Saccharomyces cerevisiae Proteins
Spinacia oleracea--enzymology
Titrimetry
Tryptophan--chemistry
Spinach chloroplast 0-acetylserine (thiol)-lyase exhibits two catalytically non-equivalent pyridoxal-5'-phosphate-containing active sites. [electronic resource] - European journal of biochemistry Feb 1996 - 272-82 p. digital
Publication Type: Journal Article; Research Support, Non-U.S. Gov't
0014-2956
10.1111/j.1432-1033.1996.00272.x doi
Amino Acid Sequence
Base Sequence
Binding Sites
Carbon-Oxygen Lyases
Catalysis
Chloroplasts--enzymology
Cysteine Synthase--chemistry
Escherichia coli--genetics
Fluorescent Dyes
Fluorometry
Genes, Plant
Genes, Synthetic
Kinetics
Lyases--chemistry
Models, Chemical
Molecular Sequence Data
Multienzyme Complexes
Protein Conformation
Pyridoxal Phosphate--chemistry
Recombinant Proteins--chemistry
Saccharomyces cerevisiae Proteins
Spinacia oleracea--enzymology
Titrimetry
Tryptophan--chemistry