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3.4.17.1: carboxypeptidase A

This is an abbreviated version!
For detailed information about carboxypeptidase A, go to the full flat file.

Word Map on EC 3.4.17.1

Reaction

release of a C-terminal amino acid, but little or no action with -Asp, -Glu, -Arg, -Lys or -Pro =

Synonyms

A-type metallocarboxypeptidase, AcCP, Anson's enzyme, ASPA, aspartoacyclase, carboxypeptidase, carboxypeptidase a, carboxypeptidase A-6, carboxypeptidase A-like activity, carboxypeptidase A1, carboxypeptidase A2, Carboxypeptidase A3, carboxypeptidase A4, carboxypeptidase vitellogenic-like, carboxypeptidase-A, carboxypolypeptidase, colon mast cell carboxypeptidase, CPA, CPA1, CPA3, CPA4, CPA6, CPAI, CPD, CPVL, EC 3.4.12.2, EC 3.4.2.1, hCPA, hCPA4, mast cell carboxypeptidase A, mast cell CPA, mast cell-CPA, mast-cell carboxypeptidase A, mast-cell CPA, MC-CP, MC-CPA, MCCPA, MCP-2, mCPA, MDCP-A1, MDCP-A2, MeCPA, MF-CPA, molting carboxypeptidase A, molting fluid carboxypeptidase A, More, Nna1/CCP1, ochratoxin A hydrolytic enzyme, PTD012, RMC-CP, vitellogenic-like carboxypeptidase

ECTree

     3 Hydrolases
         3.4 Acting on peptide bonds (peptidases)
             3.4.17 Metallocarboxypeptidases
                3.4.17.1 carboxypeptidase A

Crystallization

Crystallization on EC 3.4.17.1 - carboxypeptidase A

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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
1.25 A resolution
-
analysis of enzyme-substrate complex by difference Fourier techniques, analysis of enzyme-inhibitor complexes, mechanistic model based on crystal structure
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comparison of three carboxypeptidase A-phosphonate complexes
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complex of enzyme with the inhibitor (S)-N-sulfamoylphenylalaninecrystals are grown by the microdialysis method by equilibrating the protein-inhibitor complex in a solution of 1.2 M LiCl and 20 mM Tris-HCl buffer (pH 7.5) against a reservoir containing 0.2 M LiCl and 20 mM Tris-HCl buffer (pH 7.5)
crystal structure analysis
-
crystal structure of carboxypeptidase A complexed with D-cysteine at 1.75 A
crystal structure of complex with inactivator 2-benzyl-3-iodo-propanoic acid in two crystal forms
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crystallization reduces catalytic efficiency, abolishes substrate inhibition observed in solution
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enzyme in complex with leech carboxypeptidase inhibitor, complexing in 50 mM Tris-HCl, pH 7.5, and 100 mM NaCl, at 20°C, complex purification by gel filtration, crystallization by mixing of equal volumes of protein, containing 10-12 mg/ml protein, and reservoir solutions, the latter containing 1.5 M lithium sulfate monohydrate and 100 mM Tris, pH 8.5, sitting drop vapour diffusion method, X-ray diffraction structure determination and analysis at 2.2 A resolution
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enzyme inhibitor complexes with D-N-hydroxyaminocarbonyl phenylalanine, L-N-hydroxyaminocarbonyl phenylalanine or aminocarbonylphenylalanine
high-resolution crystallographic studies of enzyme-substrate and enzyme-inhibitor complexes
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mechanical deformation enhances catalytic activity of crystalline carboxypeptidase A
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purified enzyme in complex with the tick carboxypeptidase inhibitor, X-ray diffraction structure determination and analysis at 1.7 A resolution, comparison to the structure of unligated enzyme PDB code 1M4L, overview
relationships between enzyme structure and catalytic properties
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structural analysis of enzyme-GlyTyr complexes, design of mechanism-based inactivators based thereon
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study of pH-structure relationships
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x-ray absorption fine study of active site in solution and crystalline forms
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at 1.7 A resolution, structure is organized into a four-layer alphabetabetaalpha topology, zinc ion residing between the central beta-sheets is partially coordinated by three histidine residues
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CPA4-hexapeptide complex crystallized by sitting drop vapor diffusion method, to 1.6 A resolution
in complex with 2-benzyl-3,4-epithiobutanoic acid, hanging drop vapor diffusion method, using 20% PEG (w/v) 3350, 0.2 M NH4Cl, 0.02 M Tris pH 7.0
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in complex with inhibitor 4-methyl-2-[(2R)-thiiran-2-yl]pentanoic acid
purified recombinant CPA4 in complex with latexin, hanging drop vapour diffusion method, 0.001 ml of 7 mg/ml protein solution is mixed with 0.001 ml reservoir solution containing 40% 2-methyl-2,4-pentanediol, 0.1 M [bis(2-hydroxyethyl)amino]tris(hydroxymethyl)methane, pH 6.5, and with 0.002 ml 40% acetone, 20°C, X-ray diffraction structure determination and analysis at 1.6 A resolution
-
structural details of a true cleaved double-product complex with a hexapeptide of human ocarboxypeptidase A4 employing diffraction data to 1.6 A resolution are provided