Identification of iron ligands in tyrosine hydroxylase by mutagenesis of conserved histidinyl residues

Protein Science

Volumn 4, Issue 10, 1995, Pages 2082-2086

  Colette Daubner, S ^a   Ehrlich, Joel I ^a   Ramsey, Andrew J ^a   Fitzpatrick, Paul F ^a  

^a TEXAS A AND M UNIVERSITY   (United States)

Author keywords

active site; iron binding; mutagenesis; tyrosine hydroxylase

Indexed keywords

6 METHYLTETRAHYDROPTERIN; ALANINE; GLUTAMINE; HISTIDINE; IRON; PHENYLALANINE 4 MONOOXYGENASE; TRYPTOPHAN HYDROXYLASE; TYROSINE 3 MONOOXYGENASE;

AMINO ACID SUBSTITUTION; ARTICLE; ELECTRON SPIN RESONANCE; ENZYME ACTIVE SITE; ENZYME ACTIVITY; ENZYME KINETICS; ENZYME STRUCTURE; ENZYME SUBSTRATE COMPLEX; NONHUMAN; PRIORITY JOURNAL; RAT; SITE DIRECTED MUTAGENESIS;

AMINO ACID SEQUENCE; ANIMAL; BASE SEQUENCE; CHIMERIC PROTEINS; COMPARATIVE STUDY; CONSERVED SEQUENCE; ELECTRON SPIN RESONANCE SPECTROSCOPY; HISTIDINE; IRON; KINETICS; LIGANDS; MOLECULAR SEQUENCE DATA; MUTAGENESIS, SITE-DIRECTED; OLIGODEOXYRIBONUCLEOTIDES; POINT MUTATION; RATS; RECOMBINANT PROTEINS; SUPPORT, NON-U.S. GOV'T; SUPPORT, U.S. GOV'T, P.H.S.; TYROSINE 3-MONOOXYGENASE;

EID: 0028826732     PISSN: 09618368     EISSN: 1469896X     Source Type: Journal    
DOI: 10.1002/pro.5560041013     Document Type: Article

References (21)

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16. 1H‐NMR
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