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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
1
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pubmed:dateCreated |
1977-3-31
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pubmed:abstractText |
The distribution of bacterial L-methionine gamma-lyase (L-methionine methanethiollyase (deaminating) (EC 4.4.1.11) was investigated, and Pseudomonas ovalis (IFO 3738) was found to have the highest activity of enzyme, which was inducibly formed by addition of L-methionine to the medium. L-Methionine gamma-lyase, purified to homogeneity from Ps. ovalis, has a molecular weight of about 173 000 and consists of nonidentical subunits (mol wt: 40 000 and 48 000). The enzyme exhibits absorption maxima at 278 and 420 nm, and a shoulder around 330 nm, which are independent of the pH (6.0 to 10.0), and contains 4 mol of pyridoxal 5'-phosphate per mol of the enzyme. The formyl group of pyridoxal 5'-phosphate is bound in an aldimine linkage to the epsilon-amino group of lysine residues of the protein. The holoenzyme is resolved to the apoenzyme by incubation with hydroxylamine, and reconstituted by addition of pyridoxal 5'-phosphate. The enzyme activity is significantly affected by both carbonyl and sulfhydryl reagents. L-Methionine gamma-lyase catalyzes alpha,gamma- and alpha,beta-elimination reactions of, in addition to L-methionine, several derivatives of L-methionine and L-cysteine, e.g., L-ethionine, DL-methionine sulfone, L-homocysteine, and S-methyl-L-cysteine. The enzyme catalyzes also gamma-replacement reactions of the thiomethyl group of methionine with various alkanethiols (C2-C7), arylthio alcohols (benzenethiol and beta-naphthalenethiol) and the derivatives of ethanethiol (2-mercaptoethanol and cysteamine) to yield the corresponding S-substituted homocysteine. The thiomethyl group of S-methyl-L-cysteine also is replaced by ethanethiol to form S-ethyl-L-cysteine.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Carbon-Sulfur Lyases,
http://linkedlifedata.com/resource/pubmed/chemical/Homocysteine,
http://linkedlifedata.com/resource/pubmed/chemical/Lyases,
http://linkedlifedata.com/resource/pubmed/chemical/Macromolecular Substances,
http://linkedlifedata.com/resource/pubmed/chemical/Methionine
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pubmed:status |
MEDLINE
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pubmed:month |
Jan
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pubmed:issn |
0006-2960
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:day |
11
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pubmed:volume |
16
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
100-6
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:831771-Carbon-Sulfur Lyases,
pubmed-meshheading:831771-Homocysteine,
pubmed-meshheading:831771-Kinetics,
pubmed-meshheading:831771-Lyases,
pubmed-meshheading:831771-Macromolecular Substances,
pubmed-meshheading:831771-Magnetic Resonance Spectroscopy,
pubmed-meshheading:831771-Methionine,
pubmed-meshheading:831771-Molecular Weight,
pubmed-meshheading:831771-Oxidation-Reduction,
pubmed-meshheading:831771-Pseudomonas,
pubmed-meshheading:831771-Spectrophotometry,
pubmed-meshheading:831771-Spectrophotometry, Ultraviolet,
pubmed-meshheading:831771-Structure-Activity Relationship
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pubmed:year |
1977
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pubmed:articleTitle |
Properties of L-methionine gamma-lyase from Pseudomonas ovalis.
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pubmed:publicationType |
Journal Article
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