Characterization of Mouse Thrombin-activatable Fibrinolysis Inhibitor

Marx, Pauline F.; Wagenaar, Gerry T. M.; Reijerkerk, Arie; Tiekstra, Margriet J.; Rossum, Agnes G.S.H. van; Gebbink, Martijn F.B.G.; Meijers, Joost C. M.

doi:10.1055/s-0037-1613802

“…Currently, studies are underway to address these issues. During the preparation of our manuscript, Wagenaar et al independently reported generation of TAFI-deficient mice and observed a lack of abnormal phenotypes in their TAFI-deficient mice, consistent with our result (65).…”

Section: Figuresupporting

confidence: 91%

Thrombin-activatable fibrinolysis inhibitor (TAFI) deficiency is compatible with murine life

Nagashima¹,

Yin²,

Zhao³

et al. 2002

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Metallocarboxypeptidases

Vendrell¹,

Avilés²,

Fricker³

2004

Handbook of Metalloproteins

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Metallocarboxypeptidases (CP) catalyze the removal of C‐terminal amino acids from proteins and/or peptides. The different members of the CP family differ in their specificity for C‐terminal residues and physiological function and can be divided into two subfamilies. Members of the A/B subfamily are generally produced as proenzymes, contain an approximately 300‐residue CP catalytic domain, have greatest amino acid sequence identity to the exocrine pancreatic enzymes CPA and CPB, and prefer hydrophobic or basic residues. They function in the breakdown of peptides in food or in other physiological processes ranging from inflammation to fibrinolysis. Members of the N/E group cleave C‐terminal basic residues and are not produced as inactive proenzymes but contain an approximately 80‐residue region following the 300‐residue CP domain with structural homology to transthyretin. They act either extra‐ or intracellularly in the processing of peptide hormones and neurotransmitters and other physiologically relevant peptides. The tertiary folding of CPs corresponds to the α/β hydrolase fold and is formed by a central mixed parallel/antiparallel eight‐strand β‐sheet, with a 120° twist between the first and the last strand, over which eight α‐helices pack on both sides to form a globular molecule. All of the enzymatically active CPs bind one atom of Zn 2+ at the active site. Some members of the CP family that are inactive against standard CP substrates lack some of the cation‐binding ligands and may therefore not be able to bind the metal.

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Metallocarboxypeptidases

Vendrell¹,

Avilés²,

Fricker³

2004

Encyclopedia of Inorganic and Bioinorganic Chemistry

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Metallocarboxypeptidases (CP) catalyze the removal of C‐terminal amino acids from proteins and/or peptides. The different members of the CP family differ in their specificity for C‐terminal residues and physiological function and can be divided into two subfamilies. Members of the A/B subfamily are generally produced as proenzymes, contain an approximately 300‐residue CP catalytic domain, have greatest amino acid sequence identity to the exocrine pancreatic enzymes CPA and CPB, and prefer hydrophobic or basic residues. They function in the breakdown of peptides in food or in other physiological processes ranging from inflammation to fibrinolysis. Members of the N/E group cleave C‐terminal basic residues and are not produced as inactive proenzymes but contain an approximately 80‐residue region following the 300‐residue CP domain with structural homology to transthyretin. They act either extra‐ or intracellularly in the processing of peptide hormones and neurotransmitters and other physiologically relevant peptides. The tertiary folding of CPs corresponds to the α/β hydrolase fold and is formed by a central mixed parallel/antiparallel eight‐strand β‐sheet, with a 120° twist between the first and the last strand, over which eight α‐helices pack on both sides to form a globular molecule. All of the enzymatically active CPs bind one atom of Zn 2+ at the active site. Some members of the CP family that are inactive against standard CP substrates lack some of the cation‐binding ligands and may therefore not be able to bind the metal.

show abstract

Characterization of Mouse Thrombin-activatable Fibrinolysis Inhibitor

Cited by 34 publications

References 27 publications

Thrombin-activatable fibrinolysis inhibitor (TAFI) deficiency is compatible with murine life

Thrombin-activatable fibrinolysis inhibitor (TAFI) deficiency is compatible with murine life

Metallocarboxypeptidases

Metallocarboxypeptidases

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