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- W69633462 abstract "Since the discovery of alanine racemase (Wood and Gunsalus, 1951), there have been reports of a number of amino acid racemases. Some of them have been found to need pyridoxal phosphate as a cofactor. Certain other racemases were not activated by this cofactor. DPN has been reported to stimulate proline racemase (Stadman and Elliott, 1957) and ATP and AMP to stimulate threonine racemase (Amos, 1954). Previously one of the authors reported that the enzyme preparation of Lactobacillusfermenti ATCC 9338 was able to racemize several amino acids such as glutamic acid, aspartic acid, alanine, methionine, valine, isoleucine and phenylalanine. Pyridoxal phosphate was found to have not any stimulatory effect on the rate of glutamic acid racemization by this enzyme preparation, while the racemization of some of the other amino acids mentioned above were apparently activated by this cofactor (Tanaka,1960). Evidence for the occurence of a glutamic acid racemase was described by some investigators (Ayengar and Roberts, 1952; Narrod and Wood, 1952; Itoh, 1958). Glaser (1960) has recently reported a method for purification of glutamic acid racemase from Lactobacillusarabinosus. However, few details of the properties of glutamic acid racemase have been given up to the present. The present communication is concerned with glutamic acid racemase from L.fermenti, which was proved to be a flavoprotein." @default.
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- W69633462 date "1961-02-01" @default.
- W69633462 modified "2023-10-11" @default.
- W69633462 title "Glutamic acid racemase from Lactobacillusfermenti purification and properties" @default.
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- W69633462 doi "https://doi.org/10.1016/0006-291x(61)90358-8" @default.
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