Distal side tryptophan, tyrosine and methionine in catalase-peroxidases are covalently linked in solution

FEBS Letters

Volumn 552, Issue 2-3, 2003, Pages 135-140

  Jakopitsch, Christa ^a   Kolarich, Daniel ^a   Petutschnig, Gabriele ^a   Furtmüller, Paul Georg ^a   Obinger, Christian ^a  

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

Author keywords

Catalase activity; Catalase peroxidase; Mass spectrometry; Novel covalent bonds; Peptide mass mapping; Synechocystis PCC 6803

Indexed keywords

CATALASE; METHIONINE; PEROXIDASE; TRYPTOPHAN; TYROSINE;

AMINO ACID SUBSTITUTION; ARTICLE; COVALENT BOND; CYANOBACTERIUM; ENZYME STRUCTURE; MASS SPECTROMETRY; PEPTIDE ANALYSIS; PRIORITY JOURNAL; PROTEIN VARIANT; WILD TYPE;

SYNECHOCYSTIS; SYNECHOCYSTIS SP. PCC 6803;

EID: 0141761116     PISSN: 00145793     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0014-5793(03)00901-3     Document Type: Article

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