Methionine synthase exists in two distinct conformations that differ in reactivity toward methyltetrahydrofolate, adenosylmethionine, and flavodoxin

Biochemistry

Volumn 37, Issue 16, 1998, Pages 5372-5382

  Jarrett, Joseph T ^a,b   Huang, Sha ^a   Matthews, Rowena G ^a,c  

^a UNIVERSITY OF MICHIGAN   (United States)

^b UNIVERSITY OF PENNSYLVANIA   (United States)

^c UNIVERSITY OF MICHIGAN MEDICAL SCHOOL   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

5 METHYLTETRAHYDROFOLIC ACID; FLAVODOXIN; METHIONINE SYNTHASE; S ADENOSYLMETHIONINE;

AMINO ACID SYNTHESIS; ARTICLE; CONFORMATIONAL TRANSITION; ELECTRON TRANSPORT; ENZYME ACTIVE SITE; ENZYME ACTIVITY; ENZYME CONFORMATION; ENZYME SUBSTRATE COMPLEX; ESCHERICHIA COLI; NONHUMAN; OXIDATION; PRIORITY JOURNAL; STRUCTURE ACTIVITY RELATION;

5-METHYLTETRAHYDROFOLATE-HOMOCYSTEINE S-METHYLTRANSFERASE; ALKYL AND ARYL TRANSFERASES; BINDING, COMPETITIVE; FLAVODOXIN; GLYCINE; HISTIDINE; HYDROLYSIS; METHYLATION; MUTAGENESIS, SITE-DIRECTED; OXIDATION-REDUCTION; PROTEIN CONFORMATION; S-ADENOSYLMETHIONINE; TETRAHYDROFOLATES; TRYPSIN; VITAMIN B 12;

EID: 0032554640     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi9730893     Document Type: Article

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