Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
1973-10-15
pubmed:abstractText
Cell wall-membrane preparations of Escherichia coli, prepared by the ethylenediaminetetraacetic acid-lysozyme method, contain enzymes which catalyze the oxidation of d-alanine and, to a lesser extent, l-alanine into pyruvate and ammonia without the formation of hydrogen peroxide. The kinetic parameters were (i) pH optima of 8.3 to 8.4 for l- and d-alanine and (ii) a K(m) value of 6.6 +/- 0.2 mM for d-alanine. Several coenzymes were without effect when added to the reaction mixture. The participation of d-alanine oxidase in the oxidation of l-alanine was demonstrated. The evidence is based on (i) results of cellular fractionation; (ii) labeling experiments; (iii) inhibition studies with aminooxyacetate and cycloserine; (iv) denaturation experiments; and (v) demonstration of the presence of an active racemase.
pubmed:commentsCorrections
http://linkedlifedata.com/resource/pubmed/commentcorrection/4146873-13084603, http://linkedlifedata.com/resource/pubmed/commentcorrection/4146873-13320649, http://linkedlifedata.com/resource/pubmed/commentcorrection/4146873-13357486, http://linkedlifedata.com/resource/pubmed/commentcorrection/4146873-13549399, http://linkedlifedata.com/resource/pubmed/commentcorrection/4146873-13782323, http://linkedlifedata.com/resource/pubmed/commentcorrection/4146873-13796630, http://linkedlifedata.com/resource/pubmed/commentcorrection/4146873-14098167, http://linkedlifedata.com/resource/pubmed/commentcorrection/4146873-14389241, http://linkedlifedata.com/resource/pubmed/commentcorrection/4146873-14841188, http://linkedlifedata.com/resource/pubmed/commentcorrection/4146873-4146872, http://linkedlifedata.com/resource/pubmed/commentcorrection/4146873-4333978, http://linkedlifedata.com/resource/pubmed/commentcorrection/4146873-4387536, http://linkedlifedata.com/resource/pubmed/commentcorrection/4146873-4394638, http://linkedlifedata.com/resource/pubmed/commentcorrection/4146873-4551748, http://linkedlifedata.com/resource/pubmed/commentcorrection/4146873-4953710, http://linkedlifedata.com/resource/pubmed/commentcorrection/4146873-5325972, http://linkedlifedata.com/resource/pubmed/commentcorrection/4146873-5762454, http://linkedlifedata.com/resource/pubmed/commentcorrection/4146873-5764334
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Aug
pubmed:issn
0021-9193
pubmed:author
pubmed:issnType
Print
pubmed:volume
115
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
567-73
pubmed:dateRevised
2009-11-18
pubmed:meshHeading
pubmed-meshheading:4146873-Acetates, pubmed-meshheading:4146873-Alanine, pubmed-meshheading:4146873-Amino Acid Isomerases, pubmed-meshheading:4146873-Ammonia, pubmed-meshheading:4146873-Cell Fractionation, pubmed-meshheading:4146873-Cell Membrane, pubmed-meshheading:4146873-Cell-Free System, pubmed-meshheading:4146873-Cycloserine, pubmed-meshheading:4146873-D-Amino-Acid Oxidase, pubmed-meshheading:4146873-Deoxycholic Acid, pubmed-meshheading:4146873-Edetic Acid, pubmed-meshheading:4146873-Escherichia coli, pubmed-meshheading:4146873-Hot Temperature, pubmed-meshheading:4146873-Hydrogen-Ion Concentration, pubmed-meshheading:4146873-Muramidase, pubmed-meshheading:4146873-Oxidation-Reduction, pubmed-meshheading:4146873-Oxygen Consumption, pubmed-meshheading:4146873-Pyruvates, pubmed-meshheading:4146873-Stereoisomerism
pubmed:year
1973
pubmed:articleTitle
D-alanine oxidase from Escherichia coli: participation in the oxidation of L-alanine.
pubmed:publicationType
Journal Article