|
|
Volumn 40, Issue 42, 2001, Pages 12704-12711
|
|
MDP-1 is a new and distinct member of the haloacid dehalogenase family of aspartate-dependent phosphohydrolases
|
|
Author keywords
[No Author keywords available]
|
|
Indexed keywords
ACTIVE-SITE RESIDUES;
CATALYSIS;
CRYSTAL STRUCTURE;
HYDROPHOBICITY;
MOLECULAR WEIGHT;
ORGANIC ACIDS;
PROTEINS;
ENZYMES;
ACID PHOSPHATASE;
ASPARTIC ACID;
HALOACID DEHALOGENASE;
MAGNESIUM;
PROTEIN MDP 1;
UNCLASSIFIED DRUG;
ARTICLE;
CRYSTAL STRUCTURE;
DEPHOSPHORYLATION;
ENZYME ACTIVE SITE;
ENZYME ANALYSIS;
MASS SPECTROMETRY;
MOLECULAR WEIGHT;
NONHUMAN;
PRIORITY JOURNAL;
SEQUENCE HOMOLOGY;
SITE DIRECTED MUTAGENESIS;
AMINO ACID MOTIFS;
AMINO ACID SEQUENCE;
ANIMALS;
ASPARTIC ACID;
CATALYTIC DOMAIN;
HUMANS;
HYDROLASES;
MICE;
MOLECULAR SEQUENCE DATA;
MULTIGENE FAMILY;
MUTAGENESIS, SITE-DIRECTED;
PHOSPHOPROTEIN PHOSPHATASE;
PROTEIN STRUCTURE, TERTIARY;
PROTEIN-TYROSINE-PHOSPHATASE;
RATS;
SACCHAROMYCES CEREVISIAE;
SEQUENCE ALIGNMENT;
SEQUENCE HOMOLOGY, AMINO ACID;
EUKARYOTA;
|
|
EID: 0035940484
PISSN: 00062960
EISSN: None
Source Type: Journal
DOI: 10.1021/bi011405e Document Type: Article |
|
Times cited : (65)
|
|
References (26)
|
