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Histidine decarboxylase / Enzyme catalysis / Histidine / Enzyme / Hemoglobin / Chemistry / Biomolecules / Catalysis


doi:[removed]jmbi[removed]available online at http://www.idealibrary.com on J. Mol. Biol[removed], 727±732 pH-induced Structural Changes Regulate Histidine Decarboxylase Activity in Lactobacillus 30a
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Document Date: 2005-01-04 12:23:47


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Mixon / /

Company

HDC / Yale University Press / Patterson / RCSB Protein Data Bank / L. G. & Prozorovskii N. V. / Data Bank / Silicon Graphics / Garrett / I4122 / Coleman / /

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United States / /

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USD / /

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Event

FDA Phase / /

Facility

REFMAC.23 Model building / Jon D. Robertus* Institute of Cellular / Biochemistry University of Texas / /

IndustryTerm

active site / polysaccharide binding site / substrate-binding site / pyrÊ uvoyl / free energy difference / calciumsodium-calcium metal triad / slow cooling protocol / inactive chain / metal ions / precipitant solution / histamine product / space / functional active site / energy / /

Organization

Foundation for Research / Jon D. Robertus* Institute of Cellular and Molecular Biology / National Science Foundation / Welch Foundation / Yale University / University of Texas / Department of Chemistry / /

Person

Elisabeth Schelp / Skovoroda / Scott Worley / Arthur F. Monzingo / Jon D. Robertus / Stephen Ernst / Gallagher / /

Position

Butler / Academic Press *Corresponding author / T. D. / corresponding author / /

Product

MAPMAN25 / X-PLOR.21 To / /

ProvinceOrState

Texas / Copeland / M. B. / /

PublishedMedium

Molecular Biology / /

Technology

alpha / X-ray / directed mutagenesis / Crystallization / slow cooling protocol / /

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http /

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