Why does threonine, and not serine, function as the active site nucleophile in proteasomes?

Journal of Biological Chemistry

Volumn 275, Issue 20, 2000, Pages 14831-14837

  Kisselev, Alexei F ^a   Songyang, Zhou ^a,b,c   Goldberg, Alfred L ^a  

^a HARVARD MEDICAL SCHOOL   (United States)

^b BETH ISRAEL DEACONESS MEDICAL CENTER   (United States)

^c BAYLOR COLLEGE OF MEDICINE   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

PROTEASOME; SERINE; THREONINE;

AMINO TERMINAL SEQUENCE; ARTICLE; CATALYSIS; COMPLEX FORMATION; DNA LIBRARY; ENZYME ACTIVATION; ENZYME ACTIVE SITE; ENZYME SUBSTRATE; HYDROLYSIS; NONHUMAN; PRIORITY JOURNAL; PROTEIN ASSEMBLY; PROTEIN DEGRADATION;

NON-PROGRAMMATIC;

ADENOSINE TRIPHOSPHATASES; AMINO ACID SEQUENCE; AMINO ACID SUBSTITUTION; BINDING SITES; CYSTEINE ENDOPEPTIDASES; KINETICS; MULTIENZYME COMPLEXES; OLIGOPEPTIDES; PEPTIDE LIBRARY; PROTEASOME ENDOPEPTIDASE COMPLEX; RECOMBINANT PROTEINS; SERINE; SUBSTRATE SPECIFICITY; THERMOPLASMA; THREONINE;

ARCHAEA; THERMOPLASMA ACIDOPHILUM;

EID: 0034685889     PISSN: 00219258     EISSN: None     Source Type: Journal    
DOI: 10.1074/jbc.275.20.14831     Document Type: Article

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