A chromophore in glutamate decar☐ylase has been wrongly identified as PQQ
- 14 January 1991
- journal article
- Published by Wiley in FEBS Letters
- Vol. 278 (1) , 120-122
- https://doi.org/10.1016/0014-5793(91)80097-m
Abstract
Pyrroloquinoline quinone (PQQ) has been claimed to be a component of glutamate decar☐ylase fromEscherichia coli on the basis of a frequently used procedure in which the protein is extracted with hexanol. We demonstrate that if pyridoxal phosphate (PLP) is not added during the preparation, the apoenzyme prepared from glutamate decar☐ylase contains no chromophore absorbing above 280 nm. Full enzyme activity and the original holoenzyme spectrum are restored by the addition of PLP alone, A 340 nm-absorbing band, similar to that which prompted analysis for PQQ, is produced by exposure of the enzyme to solutions of PLPKeywords
This publication has 18 references indexed in Scilit:
- Soybean lipoxygenase‐1 is not a quinoproteinFEBS Letters, 1990
- Tryptophan decarboxylase from Catharanthus roseus is a pyridoxoquinoproteinFEBS Letters, 1989
- Determination of PQQ in quinoproteins with covalently bound cofactor and in PQQ‐derivativesFEBS Letters, 1989
- QUINOPROTEINS, ENZYMES WITH PYRROLO-QUINOLINE QUINONE AS COFACTORAnnual Review of Biochemistry, 1989
- On the biosynthesis of free and covalently bound PQQ Glutamic acid decarboxylase from Escherichia coli is a pyridoxo‐quinoproteinFEBS Letters, 1989
- Evidence for PQQ as cofactor in 3,4‐dihydroxyphenylalanine (dopa) decarboxylase of pig kidneyFEBS Letters, 1988
- Pyrroloquinoline quinone (PQQ) is the organic cofactor in soybean lipoxygenase‐1FEBS Letters, 1988
- Phenylhydrazine as probe for cofactor identification in amine oxidoreductases Evidence for PQQ as the cofactor in methylamine dehydrogenaseFEBS Letters, 1987
- A novel reaction of the coenzyme of glutamate decarboxylase with L-serine O-sulfateBiochemistry, 1982
- Chemical and physical properties of Escherichia coli glutamate decarboxylaseBiochemistry, 1970