Crystal structure of the heme d 1 biosynthesis enzyme NirE in complex with its substrate reveals new insights into the catalytic mechanism of S-adenosyl-L-methionine-dependent uroporphyrinogen III methyltransferases

Journal of Biological Chemistry

Volumn 286, Issue 30, 2011, Pages 26754-26767

  Storbeck, Sonja ^a   Saha, Sayantan ^b   Krausze, Joern ^b   Klink, Björn U ^b,c   Heinz, Dirk W ^b   Layer, Gunhild ^a  

^a TECHNICAL UNIVERSITY OF BRAUNSCHWEIG   (Germany)

^b HELMHOLTZ CENTRE FOR INFECTION RESEARCH   (Germany)

^c DUKE UNIVERSITY MEDICAL CENTER   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACID RESIDUES; ARGININE RESIDUE; BIOCHEMICAL CHARACTERIZATION; CATALYTIC MECHANISMS; COFACTORS; ENZYME-SUBSTRATE COMPLEXES; METHYL GROUP DONOR; METHYL TRANSFERS; METHYLTRANSFERASES; NITRITE REDUCTASE; PRECORRIN-2; PROTON ABSTRACTION; PSEUDOMONAS AERUGINOSA; PYRROLE RING; S ADENOSYL L METHIONINES; SITE DIRECTED MUTAGENESIS; SUBSTRATE BINDS; UROPORPHYRINOGEN III;

ALKYLATION; ARGININE; BIOCHEMISTRY; BIOSYNTHESIS; CATALYSIS; ENZYME ACTIVITY; FUNCTIONAL GROUPS; GENES; PORPHYRINS; QUANTUM CHEMISTRY; SUBSTRATES;

CRYSTAL STRUCTURE;

ADENOSYL LEVO METHIONINE DEPENDENT UROPORPHYRINOGEN III METHYLTRANSFERASE; ARGININE; BACTERIAL PROTEIN; GLUTAMIC ACID; HEME; HEME D1; HISTIDINE; METHIONINE; METHIONINE ADENOSYLTRANSFERASE; PROTEIN NIRE; S ADENOSYLHOMOCYSTEINE; S ADENOSYLMETHIONINE; UNCLASSIFIED DRUG;

AMINO ACID SEQUENCE; ARTICLE; BACTERIAL GENE; BIOCATALYSIS; BIOCHEMISTRY; BIOSYNTHESIS; CONTROLLED STUDY; CRYSTAL STRUCTURE; ENZYME BINDING; ENZYME CONFORMATION; ENZYME MECHANISM; ENZYME SUBSTRATE COMPLEX; NIRE GENE; NONHUMAN; PRIORITY JOURNAL; PSEUDOMONAS AERUGINOSA; SITE DIRECTED MUTAGENESIS;

BACTERIAL PROTEINS; CATALYSIS; CRYSTALLOGRAPHY, X-RAY; HEME; METHYLTRANSFERASES; MUTAGENESIS, SITE-DIRECTED; MUTATION, MISSENSE; PROTEIN STRUCTURE, TERTIARY; PSEUDOMONAS AERUGINOSA; UROPORPHYRINOGENS;

PSEUDOMONAS AERUGINOSA;

EID: 79960691432     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M111.239855     Document Type: Article

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