Characterisation and preliminary X-ray diffraction analysis of human pancreatic procarboxypeptidase A2

David Reverter; Isabel García-Sáez; Lluis Catasús; Josep Vendrell; Miquel Coll; Francesc X. Avilés

doi:https://doi.org/10.1016/S0014-5793(97)01476-2

Characterisation and preliminary X-ray diffraction analysis of human pancreatic procarboxypeptidase A2

David Reverter, Isabel García-Sáez, Lluis Catasús, Josep Vendrell, Miquel Coll, Francesc X. Avilés

Research output: Contribution to journal › Article › Research › peer-review

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Abstract

Human procarboxypeptidase A2 has been expressed in a Pichia pastoris heterologous system and purified by hydrophobic interaction and anion exchange chromatographies. The hydrolytic action of carboxypeptidase A2 on peptide substrates with different lengths and residues at the C-terminus was analysed, and a preference towards long substrates with aromatic amino acids in their C-terminal end, particularly tryptophan, was found; with such substrates its activity is similar or higher than that of bovine carboxypeptidase A1. Procarboxypeptidase A2 has been crystallised using a vapour diffusion approach; the crystals obtained belong to the monoclinic system, spacegroup P21, and present one procarboxypeptidase A2 molecule per asymmetric unit. The crystals diffract beyond 1.8 Å resolution and are suitable for detailed X-ray analysis.

Original language	English
Pages (from-to)	7-10
Journal	FEBS Letters
Volume	420
DOIs	https://doi.org/10.1016/S0014-5793(97)01476-2
Publication status	Published - 22 Dec 1997

Keywords

Carboxypeptidase A2
Crystallography
Proenzyme
Substrate specificity

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https://doi.org/10.1016/S0014-5793(97)01476-2

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title = "Characterisation and preliminary X-ray diffraction analysis of human pancreatic procarboxypeptidase A2",

abstract = "Human procarboxypeptidase A2 has been expressed in a Pichia pastoris heterologous system and purified by hydrophobic interaction and anion exchange chromatographies. The hydrolytic action of carboxypeptidase A2 on peptide substrates with different lengths and residues at the C-terminus was analysed, and a preference towards long substrates with aromatic amino acids in their C-terminal end, particularly tryptophan, was found; with such substrates its activity is similar or higher than that of bovine carboxypeptidase A1. Procarboxypeptidase A2 has been crystallised using a vapour diffusion approach; the crystals obtained belong to the monoclinic system, spacegroup P21, and present one procarboxypeptidase A2 molecule per asymmetric unit. The crystals diffract beyond 1.8 {\AA} resolution and are suitable for detailed X-ray analysis.",

keywords = "Carboxypeptidase A2, Crystallography, Proenzyme, Substrate specificity",

author = "David Reverter and Isabel Garc{\'i}a-S{\'a}ez and Lluis Catas{\'u}s and Josep Vendrell and Miquel Coll and Avil{\'e}s, {Francesc X.}",

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T1 - Characterisation and preliminary X-ray diffraction analysis of human pancreatic procarboxypeptidase A2

AU - Reverter, David

AU - García-Sáez, Isabel

AU - Catasús, Lluis

AU - Vendrell, Josep

AU - Coll, Miquel

AU - Avilés, Francesc X.

PY - 1997/12/22

Y1 - 1997/12/22

N2 - Human procarboxypeptidase A2 has been expressed in a Pichia pastoris heterologous system and purified by hydrophobic interaction and anion exchange chromatographies. The hydrolytic action of carboxypeptidase A2 on peptide substrates with different lengths and residues at the C-terminus was analysed, and a preference towards long substrates with aromatic amino acids in their C-terminal end, particularly tryptophan, was found; with such substrates its activity is similar or higher than that of bovine carboxypeptidase A1. Procarboxypeptidase A2 has been crystallised using a vapour diffusion approach; the crystals obtained belong to the monoclinic system, spacegroup P21, and present one procarboxypeptidase A2 molecule per asymmetric unit. The crystals diffract beyond 1.8 Å resolution and are suitable for detailed X-ray analysis.

AB - Human procarboxypeptidase A2 has been expressed in a Pichia pastoris heterologous system and purified by hydrophobic interaction and anion exchange chromatographies. The hydrolytic action of carboxypeptidase A2 on peptide substrates with different lengths and residues at the C-terminus was analysed, and a preference towards long substrates with aromatic amino acids in their C-terminal end, particularly tryptophan, was found; with such substrates its activity is similar or higher than that of bovine carboxypeptidase A1. Procarboxypeptidase A2 has been crystallised using a vapour diffusion approach; the crystals obtained belong to the monoclinic system, spacegroup P21, and present one procarboxypeptidase A2 molecule per asymmetric unit. The crystals diffract beyond 1.8 Å resolution and are suitable for detailed X-ray analysis.

KW - Carboxypeptidase A2

KW - Crystallography

KW - Proenzyme

KW - Substrate specificity

U2 - https://doi.org/10.1016/S0014-5793(97)01476-2

DO - https://doi.org/10.1016/S0014-5793(97)01476-2

M3 - Article

VL - 420

SP - 7

EP - 10

ER -

Characterisation and preliminary X-ray diffraction analysis of human pancreatic procarboxypeptidase A2

Abstract

Keywords

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