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Glutamyl-tRNA reductase activity in Bacillus subtilis is dependent on the hemA gene product

Schröder, Ingrid (author)
Hederstedt, Lars (author)
Lund University,Lunds universitet,Molekylär cellbiologi,Biologiska institutionen,Naturvetenskapliga fakulteten,Molecular Cell Biology,Department of Biology,Faculty of Science
Gamini Kannangara, C (author)
Carlsberg Research Center / Carlsberg Laboratory
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Gough, S. P. (author)
Carlsberg Research Center / Carlsberg Laboratory
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 (creator_code:org_t)
Portland Press Ltd. 1992
1992
English.
In: Biochemical Journal. - : Portland Press Ltd.. - 0264-6021 .- 1470-8728. ; , s. 843-850
  • Journal article (peer-reviewed)
Abstract Subject headings
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  • The Bacillus subtilis hemAXCDBL operon encodes enzymes for the synthesis of 5-aminolaevulinic acid via the C5 pathway (hemA and hemL) and uroporphyrinogen III (hemB, hemC and hemD). B. subtilis HemA protein (molecular mass 50 kDa) was overexpressed in hemA mutants of both Escherichia coli and B. subtilis. A mutant B. subtilis HemA protein with a Cys to Tyr change at position 105 was also overexpressed. Both wild-type and mutant HemA proteins migrated as oligomers (molecular mass greater-than-or-equal-to 230 kDa) on gel-filtration columns. All column fractions containing wild-type HemA protein had glutamyl-tRNA reductase activity. No glutamyl-tRNA reductase activity was found with the mutant HemA protein. It is concluded that the B. subtilis hemA gene product is identical to, or part of, the glutamyl-tRNA reductase of the C5 pathway.

Subject headings

NATURVETENSKAP  -- Biologi -- Mikrobiologi (hsv//swe)
NATURAL SCIENCES  -- Biological Sciences -- Microbiology (hsv//eng)
NATURVETENSKAP  -- Biologi -- Biokemi och molekylärbiologi (hsv//swe)
NATURAL SCIENCES  -- Biological Sciences -- Biochemistry and Molecular Biology (hsv//eng)

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Schröder, Ingrid
Hederstedt, Lars
Gamini Kannangar ...
Gough, S. P.
About the subject
NATURAL SCIENCES
NATURAL SCIENCES
and Biological Scien ...
and Microbiology
NATURAL SCIENCES
NATURAL SCIENCES
and Biological Scien ...
and Biochemistry and ...
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Biochemical Jour ...
By the university
Lund University

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