Literature DB >> 6688526

The occurrence of beta-hydroxyaspartic acid in the vitamin K-dependent blood coagulation zymogens.

B A McMullen, K Fujikawa, W Kisiel.   

Abstract

Previous work has shown that two vitamin K-dependent plasma zymogens, factor X and protein C, each contain one residue of erythro-beta-hydroxyaspartic acid. In the present study, prothrombin, factor VII and factor IX were subjected to amino acid analyses for beta-hydroxyaspartic acid. Factor IX and factor VII each contain one residue of erythro-beta-hydroxyaspartic acid. Edman sequence analyses revealed that this residue occurs at position 64 in human and bovine factor IX. Inasmuch as the nucleotide sequence codes for aspartic acid at this position, it appears highly likely that beta-hydroxyaspartic acid is formed in these proteins by a post-translational hydroxylation of aspartic acid. In contrast, neither human nor bovine prothrombin contain beta-hydroxyaspartic acid.

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Year:  1983        PMID: 6688526     DOI: 10.1016/0006-291x(83)90961-0

Source DB:  PubMed          Journal:  Biochem Biophys Res Commun        ISSN: 0006-291X            Impact factor:   3.575


  18 in total

Review 1.  The interaction between complement component C4b-binding protein and the vitamin K-dependent protein S forms a link between blood coagulation and the complement system.

Authors:  M Hessing
Journal:  Biochem J       Date:  1991-08-01       Impact factor: 3.857

2.  Complete amino acid sequence of the A chain of human complement-classical-pathway enzyme C1r.

Authors:  G J Arlaud; A C Willis; J Gagnon
Journal:  Biochem J       Date:  1987-02-01       Impact factor: 3.857

3.  Thrombin activation of protein C requires prior processing by a liver proprotein convertase.

Authors:  Rachid Essalmani; Delia Susan-Resiga; Johann Guillemot; Woojin Kim; Vatsal Sachan; Zuhier Awan; Ann Chamberland; Marie-Claude Asselin; Kévin Ly; Roxane Desjardins; Robert Day; Annik Prat; Nabil G Seidah
Journal:  J Biol Chem       Date:  2017-05-03       Impact factor: 5.157

4.  Aspartyl beta-hydroxylase: in vitro hydroxylation of a synthetic peptide based on the structure of the first growth factor-like domain of human factor IX.

Authors:  R S Gronke; W J VanDusen; V M Garsky; J W Jacobs; M K Sardana; A M Stern; P A Friedman
Journal:  Proc Natl Acad Sci U S A       Date:  1989-05       Impact factor: 11.205

5.  Characterization of a cDNA coding for human factor X.

Authors:  S P Leytus; D W Chung; W Kisiel; K Kurachi; E W Davie
Journal:  Proc Natl Acad Sci U S A       Date:  1984-06       Impact factor: 11.205

6.  Characterization of a cDNA coding for human protein C.

Authors:  D Foster; E W Davie
Journal:  Proc Natl Acad Sci U S A       Date:  1984-08       Impact factor: 11.205

7.  Molecular basis of hemophilia B: a defective enzyme due to an unprocessed propeptide is caused by a point mutation in the factor IX precursor.

Authors:  D L Diuguid; M J Rabiet; B C Furie; H A Liebman; B Furie
Journal:  Proc Natl Acad Sci U S A       Date:  1986-08       Impact factor: 11.205

8.  The interaction of bovine factor IX, its activation intermediate, factor IX alpha, and its activation products, factor IXa alpha and factor IXa beta, with acidic phospholipid vesicles of various compositions.

Authors:  J M Beals; F J Castellino
Journal:  Biochem J       Date:  1986-06-15       Impact factor: 3.857

9.  Hydroxylation of aspartic acid in domains homologous to the epidermal growth factor precursor is catalyzed by a 2-oxoglutarate-dependent dioxygenase.

Authors:  J Stenflo; E Holme; S Lindstedt; N Chandramouli; L H Huang; J P Tam; R B Merrifield
Journal:  Proc Natl Acad Sci U S A       Date:  1989-01       Impact factor: 11.205

10.  Characterization of a cDNA coding for human factor VII.

Authors:  F S Hagen; C L Gray; P O'Hara; F J Grant; G C Saari; R G Woodbury; C E Hart; M Insley; W Kisiel; K Kurachi
Journal:  Proc Natl Acad Sci U S A       Date:  1986-04       Impact factor: 11.205

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