Characterization of the smtA gene encoding an S-adenosylmethionine-dependent methyltransferase of Escherichia coli
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The Escherichia coli cysG gene encodes S-adenosylmethionine-dependent uroporphyrinogen III methylase.
The Escherichia coli cysG gene was successfully subcloned and over-expressed to produce a 52 kDa protein that was purified to homogeneity. This protein was shown to catalyse the S-adenosylmethionine-dependent methylation of uroporphyrinogen III to give a product identified as sirohydrochlorin on the basis of its absorption spectra, incorporation of 14C label from S-adenosyl[Me-14C]methionine an...
متن کاملThe sequence of metK, the structural gene for S-adenosylmethionine synthetase in Escherichia coli.
The DNA sequence of the Escherichia coli metK gene has been determined. Protein sequence data for purified S-adenosylmethionine synthetase have also been obtained and confirm that metK is the structural gene for S-adenosylmethionine synthetase in E. coli. The sequence of the amino-terminal 35 residues of purified S-adenosylmethionine synthetase localizes the beginning of the coding region of th...
متن کاملRegulation of S-adenosylmethionine synthetase in Escherichia coli.
Addition of methionine to the growth medium of Escherichia coli K-12 leads to a reduction in the specific activity of S-adenosylmethionine (SAM) synthetase. Thus the enzyme appears to be repressible rather than inducible. Mutant strains (probably metJ(-)) are constitutive for SAM synthetase as well as for the methionine biosynthetic enzymes, suggesting that the regulatory systems for these enzy...
متن کاملCloning and characterization of the metE gene encoding S-adenosylmethionine synthetase from Bacillus subtilis.
The metE gene, encoding S-adenosylmethionine synthetase (EC 2.5.1.6) from Bacillus subtilis, was cloned in two steps by normal and inverse PCR. The DNA sequence of the metE gene contains an open reading frame which encodes a 400-amino-acid sequence that is homologous to other known S-adenosylmethionine synthetases. The cloned gene complements the metE1 mutation and integrates at or near the chr...
متن کاملCharacterization of the aes gene of Escherichia coli encoding an enzyme with esterase activity.
malQ mutants of Escherichia coli lacking amylomaltase cannot grow on maltose. They express the maltose system constitutively and are sensitive to maltose when grown on another carbon source. In an attempt to isolate a multicopy suppressor that would result in growth on maltose, we transformed a malQ mutant with a gene bank of E. coli DNA which had been digested with Sau3a and cloned in pBR322. ...
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ژورنال
عنوان ژورنال: FEMS Microbiology Letters
سال: 1995
ISSN: 0378-1097
DOI: 10.1016/0378-1097(95)00335-3