Crystal structure of Klebsiella sp. ASR1 phytase suggests substrate binding to a preformed active site that meets the requirements of a plant rhizosphere enzyme

FEBS Journal

Volumn 277, Issue 5, 2010, Pages 1284-1296

  Böhm, Kerstin ^a   Herter, Thomas ^b   Müller, Jürgen J ^a   Borriss, Rainer ^b   Heinemann, Udo ^a,c  

^a MAX DELBRÜCK CENTER FOR MOLECULAR MEDICINE   (Germany)

^b HUMBOLDT UNIVERSITY   (Germany)

^c FREIE UNIVERSITÄT BERLIN   (Germany)

Author keywords

Dephosphorylation; Phytase; Plant rhizosphere enzyme; Preformed substrate binding site; Protein structure

Indexed keywords

ACID PHOSPHATASE PROSTATE ISOENZYME; ASR1 PHYTASE; ENZYME; PHYTASE; PHYTATE; PHYTIC ACID; POLYPEPTIDE; SCAVENGER; SULFATE; UNCLASSIFIED DRUG;

ARTICLE; BINDING SITE; CELL PH; CRYSTAL STRUCTURE; DEGRADATION; ESCHERICHIA COLI; HABITAT; KLEBSIELLA; MUTANT; NONHUMAN; PLANT; PRIORITY JOURNAL; PROTEIN STRUCTURE; RHIZOSPHERE;

6-PHYTASE; AMINO ACID SEQUENCE; CATALYTIC DOMAIN; CLONING, MOLECULAR; CRYSTALLOGRAPHY, X-RAY; HYDROGEN BONDING; KLEBSIELLA; MODELS, MOLECULAR; MOLECULAR CONFORMATION; MOLECULAR STRUCTURE; PROTEIN BINDING; RHIZOME; SEQUENCE ALIGNMENT; SUBSTRATE SPECIFICITY;

ESCHERICHIA COLI; KLEBSIELLA; KLEBSIELLA SP.;

EID: 76349089524     PISSN: 1742464X     EISSN: 17424658     Source Type: Journal    
DOI: 10.1111/j.1742-4658.2010.07559.x     Document Type: Article

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