Tautomeric state of α-sarcin histidines. Nδ tautomers are a common feature in the active site of extracellular microbial ribonucleases

FEBS Letters

Volumn 534, Issue 1-3, 2003, Pages 197-201

  Pérez Cañadilllas, José Manuel ^a,c   García Mayoral, Ma Flor ^a   Laurents, Douglas V ^a   Martínez del Pozo, Alvaro ^b   Gavilanes, José G ^b   Rico, Manuel ^a   Bruix, Marta ^a  

^a INSTITUTO DE QUÍMICA FÍSICA ROCASOLANO   (Spain)

^b UNIVERSIDAD COMPLUTENSE DE MADRID   (Spain)

^c MRC LABORATORY OF MOLECULAR BIOLOGY   (United Kingdom)

Author keywords

Histidine tautomer; pKa; Ribonuclease; Ribotoxin; Sarcin

Indexed keywords

ALPHA SARCIN; HISTIDINE 104; HISTIDINE 137; HISTIDINE 35; HISTIDINE 36; HISTIDINE 50; HISTIDINE 82; HISTIDINE 92; HISTIDINE DERIVATIVE; IMIDAZOLE DERIVATIVE; MICROBIAL ENZYME; PEPTIDE; RIBONUCLEASE; RIBONUCLEASE T1; TOXIN; UNCLASSIFIED DRUG;

ARTICLE; CHEMONUCLEOLYSIS; CRYSTAL STRUCTURE; ENZYME ACTIVE SITE; ENZYME ACTIVITY; ENZYME ANALYSIS; NONHUMAN; NUCLEAR MAGNETIC RESONANCE IMAGING; PREDICTION; PRIORITY JOURNAL; PROTEIN FAMILY; PROTEIN FUNCTION; PROTEIN STRUCTURE;

EID: 0037448413     PISSN: 00145793     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0014-5793(02)03844-9     Document Type: Article

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