Crystal structure and substrate specificity of plant adenylate isopentenyltransferase from Humulus lupulus: Distinctive binding affinity for purine and pyrimidine nucleotides

Nucleic Acids Research

Volumn 38, Issue 5, 2009, Pages 1738-1748

  Chu, Hsing Mao ^a,b   Ko, Tzu Ping ^b   Wang, Andrew H J ^a,b  

^a NATIONAL TAIWAN UNIVERSITY   (Taiwan)

^b INSTITUTE OF BIOLOGICAL CHEMISTRY   (Taiwan)

Author keywords

[No Author keywords available]

Indexed keywords

ADENOSINE DIPHOSPHATE; ADENOSINE TRIPHOSPHATE; ADENYLATE ISOPENTENYLTRANSFERASE; ALANINE AMINOTRANSFERASE; ASPARTIC ACID; CYTIDINE TRIPHOSPHATE; LYSINE; PURINE NUCLEOTIDE; PYRIMIDINE NUCLEOTIDE; TRANSFER RNA; TRANSFERASE; UNCLASSIFIED DRUG; URIDINE TRIPHOSPHATE;

ARTICLE; BINDING AFFINITY; CONTROLLED STUDY; CRYSTAL STRUCTURE; ENZYME SPECIFICITY; HUMULUS LUPULUS; ISOTHERMAL TITRATION CALORIMETRY; NONHUMAN; PRIORITY JOURNAL; PROTEIN INTERACTION; RHIZOBIUM; SACCHAROMYCES CEREVISIAE; CHEMICAL STRUCTURE; CHEMISTRY; ENZYME ACTIVE SITE; ENZYMOLOGY; HUMULUS; METABOLISM; X RAY CRYSTALLOGRAPHY;

AGROBACTERIUM; BACTERIA (MICROORGANISMS); HUMULUS LUPULUS;

ALKYL AND ARYL TRANSFERASES; ASPARTIC ACID; CATALYTIC DOMAIN; CRYSTALLOGRAPHY, X-RAY; HUMULUS; MODELS, MOLECULAR; PURINE NUCLEOTIDES; PYRIMIDINE NUCLEOTIDES; RHIZOBIUM; RNA, TRANSFER; SUBSTRATE SPECIFICITY;

EID: 77950472622     PISSN: 03051048     EISSN: 13624962     Source Type: Journal    
DOI: 10.1093/nar/gkp1093     Document Type: Article

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