Structure-function relationships in methionine adenosyltransferases

Cellular and Molecular Life Sciences

Volumn 66, Issue 4, 2009, Pages 636-648

  Markham, G D ^a   Pajares, M A ^b  

^a FOX CHASE CANCER CENTER   (United States)

^b INSTITUTO DE INVESTIGACIONES BIOMÉDICAS ALBERTO SOLS   (Spain)

Author keywords

Crystal structure; Folding; Hepatic disease; Methionine adenosyltransferase; Mutants; Reaction mechanism; S adenosylmethionine synthetase

Indexed keywords

METHIONINE ADENOSYLTRANSFERASE;

CATALYSIS; CHEMICAL MODIFICATION; COMPLEX FORMATION; CRYSTAL STRUCTURE; ENZYME STRUCTURE; HUMAN; MUTAGENESIS; NONHUMAN; OLIGOMERIZATION; PREDICTION; PROTEIN CONFORMATION; PROTEIN DOMAIN; PROTEIN EXPRESSION; PROTEIN FOLDING; PROTEIN FUNCTION; REVIEW; STRUCTURE ACTIVITY RELATION;

ANIMALS; CRYSTALLOGRAPHY, X-RAY; HUMANS; ISOENZYMES; METHIONINE; METHIONINE ADENOSYLTRANSFERASE; MODELS, MOLECULAR; PROTEIN CONFORMATION; PROTEIN FOLDING; PROTEIN SUBUNITS; S-ADENOSYLMETHIONINE; STRUCTURE-ACTIVITY RELATIONSHIP;

EUKARYOTA;

EID: 60149109785     PISSN: 1420682X     EISSN: 15691632     Source Type: Journal    
DOI: 10.1007/s00018-008-8516-1     Document Type: Review

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