Multidomain human peroxidasin 1 is a highly glycosylated and stable homotrimeric high spin ferric peroxidase

Journal of Biological Chemistry

Volumn 290, Issue 17, 2015, Pages 10876-10890

  Soudi, Monika ^a   Paumann Page, Martina ^a   Delporte, Cedric ^b   Pirker, Katharina F ^a   Bellei, Marzia ^c   Edenhofer, Eva ^a   Stadlmayr, Gerhard ^a   Battistuzzi, Gianantonio ^c   Boudjeltia, Karim Zouaoui ^b   Furtmüller, Paul G ^a   Van Antwerpen, Pierre ^b   Obinger, Christian ^a  

^a UNIVERSITY OF NATURAL RESOURCES AND LIFE SCIENCES   (Austria)

^b UNIVERSITÉ LIBRE DE BRUXELLES   (Belgium)

^c UNIVERSITY OF MODENA AND REGGIO EMILIA   (Italy)

Author keywords

[No Author keywords available]

Indexed keywords

CATALYTIC OXIDATION; CELL CULTURE; PORPHYRINS;

BIOPHYSICAL PROPERTIES; CATALYTIC EFFICIENCIES; COVALENTLY BOUND; N-GLYCOSYLATION SITES; OLIGOMERIC STRUCTURE; SEQUENCE HOMOLOGY; STANDARD REDUCTION POTENTIALS; STRUCTURAL REINFORCEMENT;

COLLAGEN;

BROMIDE; COLLAGEN TYPE 4; HUMAN PEROXIDASIN 1; PEROXIDASE; UNCLASSIFIED DRUG; INTERLEUKIN 1 RECEPTOR; IRON; PXDN PROTEIN, HUMAN; TUMOR ANTIGEN;

AMINO ACID COMPOSITION; AMINO ACID SEQUENCE; ARTICLE; CONCENTRATION (PARAMETERS); CONFORMATIONAL TRANSITION; CONTROLLED STUDY; COVALENT BOND; ENZYME ACTIVE SITE; ENZYME SUBUNIT; HUMAN; MOLECULAR WEIGHT; OLIGOMERIZATION; OXIDATION; PRIORITY JOURNAL; PROTEIN BINDING; PROTEIN CROSS LINKING; PROTEIN DEPLETION; PROTEIN DOMAIN; PROTEIN EXPRESSION; PROTEIN FUNCTION; PROTEIN GLYCOSYLATION; PROTEIN SECONDARY STRUCTURE; REDUCTION; REDUCTION POTENTIAL; SEQUENCE ANALYSIS; SEQUENCE HOMOLOGY; STRUCTURE ANALYSIS; CATALYSIS; CHEMISTRY; GENETICS; GLYCOSYLATION; HEK293 CELL LINE; METABOLISM; OXIDATION REDUCTION REACTION; PROTEIN TERTIARY STRUCTURE; STRUCTURE ACTIVITY RELATION;

ANTIGENS, NEOPLASM; CATALYSIS; COLLAGEN TYPE IV; GLYCOSYLATION; HEK293 CELLS; HUMANS; IRON; OXIDATION-REDUCTION; PROTEIN STRUCTURE, TERTIARY; RECEPTORS, INTERLEUKIN-1; STRUCTURE-ACTIVITY RELATIONSHIP;

EID: 84928403603     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M114.632273     Document Type: Article

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