4.1.3.38: aminodeoxychorismate lyase
This is an abbreviated version!
For detailed information about aminodeoxychorismate lyase, go to the full flat file.
Reaction
Synonyms
4-amino-4-deoxychorismate lyase, Abz2, ADC lyase, ADCL, ADCS, aminodeoxychorismate lyase, aminodeoxychorismate synthase, enzyme X, PabC, PabC-1, PabC-2, TTHA0621 protein
ECTree
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General Information on EC 4.1.3.38 - aminodeoxychorismate lyase
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GENERAL INFORMATION 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
evolution
metabolism
physiological function
the enzyme is active in folate biosynthesis and essential for the cell growth of the pathogen
additional information
evolution
4-amino-4-deoxychorismate lyases can be divided into two classes of dimeric and monomeric enzyme, respectively
evolution
structure comparisons with related enzymes, overview. PabC enzymes can be classified into two groups depending upon whether an active site and structurally conserved tyrosine is provided from the polypeptide that mainly forms an active site or from the partner subunit in the dimeric assembly
additional information
structure-activity relationship of PabC, ligand binding modeling and reaction mechanism, overview. No structure of PabC in complex with ligands is achieved, but a computational model of the catalytic intermediate docked into the enzyme active site is generated. A conserved tyrosine helps to create a hydrophobic wall on one side of the active site that provides important interactions to bind the catalytic intermediate, but it does not appear to participate in interactions with the C atom that undergoes an sp2 to sp3 conversion as pyruvate is produced. An active site threonine hydroxyl contributes a proton used in the reduction of the substrate methylene to pyruvate methyl in the final stage of the mechanism
additional information
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structure-activity relationship of PabC, ligand binding modeling and reaction mechanism, overview. No structure of PabC in complex with ligands is achieved, but a computational model of the catalytic intermediate docked into the enzyme active site is generated. A conserved tyrosine helps to create a hydrophobic wall on one side of the active site that provides important interactions to bind the catalytic intermediate, but it does not appear to participate in interactions with the C atom that undergoes an sp2 to sp3 conversion as pyruvate is produced. An active site threonine hydroxyl contributes a proton used in the reduction of the substrate methylene to pyruvate methyl in the final stage of the mechanism
additional information
the catalytic residue Lys251 covalently binds the cofactor pyridoxal 5'-phosphate
additional information
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the catalytic residue Lys251 covalently binds the cofactor pyridoxal 5'-phosphate
