000 01470 a2200373 4500
005 20250516155024.0
264 0 _c20131101
008 201311s 0 0 eng d
022 _a1083-351X
024 7 _a10.1074/jbc.M113.486613
_2doi
040 _aNLM
_beng
_cNLM
100 1 _aMainprize, Iain L
245 0 0 _aThe UDP-glucose dehydrogenase of Escherichia coli K-12 displays substrate inhibition by NAD that is relieved by nucleotide triphosphates.
_h[electronic resource]
260 _bThe Journal of biological chemistry
_cAug 2013
300 _a23064-74 p.
_bdigital
500 _aPublication Type: Journal Article; Research Support, Non-U.S. Gov't
650 0 4 _aAdenosine Triphosphate
_xchemistry
650 0 4 _aAmino Acid Substitution
650 0 4 _aEscherichia coli K12
_xenzymology
650 0 4 _aEscherichia coli Proteins
_xchemistry
650 0 4 _aKinetics
650 0 4 _aMutagenesis, Site-Directed
650 0 4 _aMutation, Missense
650 0 4 _aNAD
_xchemistry
650 0 4 _aPolysaccharides
_xbiosynthesis
650 0 4 _aUridine Diphosphate Glucose Dehydrogenase
_xantagonists & inhibitors
650 0 4 _aVirulence Factors
_xchemistry
700 1 _aBean, Jordan D
700 1 _aBouwman, Catrien
700 1 _aKimber, Matthew S
700 1 _aWhitfield, Chris
773 0 _tThe Journal of biological chemistry
_gvol. 288
_gno. 32
_gp. 23064-74
856 4 0 _uhttps://doi.org/10.1074/jbc.M113.486613
_zAvailable from publisher's website
999 _c22859044
_d22859044