Structural basis for dual specificity of yeast N-terminal amidase in the N-end rule pathway

Proceedings of the National Academy of Sciences of the United States of America

Volumn 113, Issue 44, 2016, Pages 12438-12443

  Kim, Min Kyung ^a   Oh, Sun Joo ^a   Lee, Byung Gil ^a,b   Song, Hyun Kyu ^a  

^a Korea University   (South Korea)

^b MRC LABORATORY OF MOLECULAR BIOLOGY   (United Kingdom)

Author keywords

Dual specificity; N end rule; Nitrilase superfamily; Nta1

Indexed keywords

AMIDASE; ASPARTIC ACID; GLUTAMINE; N TERMINAL AMIDASE; UNCLASSIFIED DRUG; ASPARAGINE; NTA1 PROTEIN, S CEREVISIAE; PEPTIDE; SACCHAROMYCES CEREVISIAE PROTEIN;

AMINO TERMINAL SEQUENCE; BINDING AFFINITY; CONFERENCE PAPER; CRYSTAL STRUCTURE; DEAMINATION; ENZYME BINDING; ENZYME SPECIFICITY; ENZYME STRUCTURE; HYDROGEN BOND; MUTAGENESIS; NONHUMAN; PRIORITY JOURNAL; YEAST; AMINO ACID SEQUENCE; CHEMISTRY; ENZYME ACTIVE SITE; ENZYMOLOGY; GENETICS; KINETICS; METABOLISM; MOLECULAR MODEL; PROTEIN CONFORMATION; PROTEIN DEGRADATION; SACCHAROMYCES CEREVISIAE; SEQUENCE HOMOLOGY; X RAY CRYSTALLOGRAPHY;

AMIDOHYDROLASES; AMINO ACID SEQUENCE; ASPARAGINE; CATALYTIC DOMAIN; CRYSTALLOGRAPHY, X-RAY; GLUTAMINE; HYDROGEN BONDING; KINETICS; MODELS, MOLECULAR; PEPTIDES; PROTEIN CONFORMATION; PROTEOLYSIS; SACCHAROMYCES CEREVISIAE; SACCHAROMYCES CEREVISIAE PROTEINS; SEQUENCE HOMOLOGY, AMINO ACID; SUBSTRATE SPECIFICITY;

EID: 84994242315     PISSN: 00278424     EISSN: 10916490     Source Type: Journal    
DOI: 10.1073/pnas.1612620113     Document Type: Article

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