The modular structure of ThDP-dependent enzymes

Proteins: Structure, Function and Bioinformatics

Volumn 82, Issue 10, 2014, Pages 2523-2537

  Vogel, Constantin ^a   Pleiss, Jürgen ^a  

^a UNIVERSITY OF STUTTGART   (Germany)

Author keywords

Architecture; Domain; Modularity; PP; PYR; Pyrimidine; Pyrophosphate; Rearrangement; Rewiring; Structural conservation; TEED; Thiamine diphosphate

Indexed keywords

2 OXOACID DEHYDROGENASE; CARBOXYLASE; CARBOXYLYASE; COCARBOXYLASE; GLUTAMIC ACID; GLYCINE; HOMODIMER; MONOMER; OXIDOREDUCTASE; OXOGLUTARATE DEHYDROGENASE; SULFOPYRUVATE DECARBOXYLASE; THIAMINE DIPHOSPHATE DEPENDENT ENZYME; UNCLASSIFIED DRUG; ENZYME; INORGANIC PYROPHOSPHATASE; PYRIMIDINE; PYRIMIDINE DERIVATIVE;

AMINO TERMINAL SEQUENCE; ARTICLE; ENZYME ACTIVE SITE; ENZYME STRUCTURE; PRIORITY JOURNAL; PROTEIN FAMILY; PROTEIN SECONDARY STRUCTURE; SEQUENCE HOMOLOGY; BINDING SITE; CHEMICAL STRUCTURE; CHEMISTRY; HUMAN; METABOLISM; MOLECULAR EVOLUTION; PROTEIN CONFORMATION;

BINDING SITES; CARBOXY-LYASES; CATALYTIC DOMAIN; ENZYMES; EVOLUTION, MOLECULAR; HUMANS; MODELS, MOLECULAR; PROTEIN CONFORMATION; PYRIMIDINES; PYROPHOSPHATASES; THIAMINE PYROPHOSPHATE;

EID: 84919700163     PISSN: 08873585     EISSN: 10970134     Source Type: Journal    
DOI: 10.1002/prot.24615     Document Type: Article

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