Structural and functional insights into the regulation of helicobacter pylori arginase activity by an evolutionary nonconserved motif

Biochemistry

Volumn 52, Issue 3, 2013, Pages 508-519

  Srivastava, Abhishek ^a   Meena, Shiv Kumar ^a   Alam, Mashkoor ^a   Nayeem, Shahid M ^b   Deep, Shashank ^b   Sau, Apurba Kumar ^a  

^a NATIONAL INSTITUTE OF IMMUNOLOGY   (India)

^b INDIAN INSTITUTE OF TECHNOLOGY DELHI   (India)

Author keywords

[No Author keywords available]

Indexed keywords

AROMATIC RESIDUES; CATALYTIC FUNCTIONS; HELICAL STRUCTURES; HELICOBACTER PYLORI; HELIX STRUCTURES; KINETIC ASSAY; METAL RETENTION; MOLECULAR DYNAMICS SIMULATIONS; MUTATIONAL ANALYSIS; POLYAMINES; SIMULATION STUDIES; SITE DIRECTED MUTAGENESIS;

CATALYSIS; ENZYMES; MOLECULAR DYNAMICS; RNA; UREA;

STABILIZATION;

ARGINASE; ASPARTIC ACID; CYSTEINE; GLUTAMIC ACID; TRYPTOPHAN;

ARTICLE; CATALYSIS; CHEMICAL STRUCTURE; CIRCULAR DICHROISM; DENATURATION; ENZYME ACTIVITY; ESCHERICHIA COLI; GENETIC CONSERVATION; HEAT; HELICOBACTER PYLORI; KINETICS; METAL BINDING; MOLECULAR DYNAMICS; NONHUMAN; PRIORITY JOURNAL; PROTEIN STABILITY; SITE DIRECTED MUTAGENESIS; STEADY STATE; THERMOSTABILITY;

AMINO ACID SUBSTITUTION; ARGINASE; ASPARTIC ACID; BACTERIAL PROTEINS; BIOCATALYSIS; CIRCULAR DICHROISM; COBALT; ENZYME STABILITY; HELICOBACTER PYLORI; HOT TEMPERATURE; KINETICS; MANGANESE; MOLECULAR DOCKING SIMULATION; MUTAGENESIS, SITE-DIRECTED; MUTANT PROTEINS; PEPTIDE FRAGMENTS; PROTEIN DENATURATION; PROTEIN INTERACTION DOMAINS AND MOTIFS; RECOMBINANT PROTEINS; TRYPTOPHAN;

HELICOBACTER PYLORI;

EID: 84872782242     PISSN: 00062960     EISSN: 15204995     Source Type: Journal    
DOI: 10.1021/bi301421v     Document Type: Article

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