Apple 1-aminocyclopropane-1-carboxylate synthase in complex with the inhibitor L-aminoethoxyvinylglycine. Evidence for a ketimine intermediate

scientific article

Apple 1-aminocyclopropane-1-carboxylate synthase in complex with the inhibitor L-aminoethoxyvinylglycine. Evidence for a ketimine intermediate is …
instance of (P31):
scholarly articleQ13442814

External links are
P356DOI10.1074/JBC.M208427200
P698PubMed publication ID12228256

P50authorGuido CapitaniQ28468973
P2093author name stringMarkus G Grütter
Darla L McCarthy
Heinz Gut
Jack F Kirsch
P2860cites workImproved methods for building protein models in electron density maps and the location of errors in these modelsQ26776980
PROCHECK: a program to check the stereochemical quality of protein structuresQ26778411
Structure of 1-aminocyclopropane-1-carboxylate synthase, a key enzyme in the biosynthesis of the plant hormone ethyleneQ27620804
Crystal structure of cystalysin from Treponema denticola: a pyridoxal 5'-phosphate-dependent protein acting as a haemolytic enzymeQ27625168
Crystal structures of 1-aminocyclopropane-1-carboxylate (ACC) synthase in complex with aminoethoxyvinylglycine and pyridoxal-5'-phosphate provide new insight into catalytic mechanismsQ27632861
Slow-binding inhibition of Escherichia coli cystathionine beta-lyase by L-aminoethoxyvinylglycine: a kinetic and X-ray studyQ27747982
Errors in protein structuresQ27860776
The CCP4 suite: programs for protein crystallographyQ27861090
LIGPLOT: a program to generate schematic diagrams of protein-ligand interactionsQ27861128
L-Vinylglycine is an alternative substrate as well as a mechanism-based inhibitor of 1-aminocyclopropane-1-carboxylate synthaseQ28372437
AMoRe: an automated package for molecular replacementQ29642803
The reaction catalyzed by Escherichia coli aspartate aminotransferase has multiple partially rate-determining steps, while that catalyzed by the Y225F mutant is dominated by ketimine hydrolysisQ34376614
Expression of apple 1-aminocyclopropane-1-carboxylate synthase in Escherichia coli: kinetic characterization of wild-type and active-site mutant forms.Q35983113
Glutamate 47 in 1-aminocyclopropane-1-carboxylate synthase is a major specificity determinantQ43759595
Kinetic and spectroscopic investigations of wild-type and mutant forms of apple 1-aminocyclopropane-1-carboxylate synthaseQ46152484
Accurate bond and angle parameters for X-ray protein structure refinementQ56485700
Antifungal antibiotics and Siba inhibit 1-aminocyclopropane-1-carboxylic acid synthase activityQ70989917
Model-free methods of analyzing domain motions in proteins from simulation: a comparison of normal mode analysis and molecular dynamics simulation of lysozymeQ73205389
P433issue51
P407language of work or nameEnglishQ1860
P304page(s)49735-42
P577publication date2002-12-20
P1433published inJournal of Biological ChemistryQ867727
P1476titleApple 1-aminocyclopropane-1-carboxylate synthase in complex with the inhibitor L-aminoethoxyvinylglycine. Evidence for a ketimine intermediate
P478volume277