Inversion of the allosteric response of Escherichia coli glucosamine-6-P deaminase to N-acetylglucosamine 6-P, by single amino acid replacements

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Fältnamn	Indikatorer	Metadata
000		02825naa a2200313 4500
001		oai:DiVA.org:umu-156785
003		SwePub
008		190226s2004 \| \|\|\|\|\|\|\|\|\|\|\|000 \|\|eng\|
024	7	a https://urn.kb.se/resolve?urn=urn:nbn:se:umu:diva-1567852 URI
024	7	a https://doi.org/10.1016/j.abb.2003.09.0412 DOI
040		a (SwePub)umu
041		a engb eng
042		9 SwePub
072	7	a ref2 swepub-contenttype
072	7	a art2 swepub-publicationtype
100	1	a Cisneros, David A.u Laboratorio de Fisicoquímica e Ingeniería de Proteínas, Departamento de Bioquímica, Facultad de Medicina, Universidad Nacional Autónoma de México (UNAM), P.O. Box 70-159, Mexico City, D.F, 04510, Mexico4 aut0 (Swepub:umu)daci0002
245	1 0	a Inversion of the allosteric response of Escherichia coli glucosamine-6-P deaminase to N-acetylglucosamine 6-P, by single amino acid replacements
264	1	b Elsevier BV,c 2004
338		a print2 rdacarrier
520		a Amino acid replacements in the active site of glucosamine-6-P deaminase from Escherichia coli (GlcN6P deaminase, EC 3.5.99.6) involving the residues D141 and E148 produce atypical allosteric kinetics. These residues are located in the chain segment 139-156 which is part of the active site and which also forms several intersubunit contacts close to the allosteric site. In the D141N and E148Q mutant forms of this deaminase, there is an inversion of the effect of its physiological allosteric effector, N-acetylglucosamine 6-P, which becomes an inhibitor at substrate concentrations above a critical value. For both mutants, this particular point appears at low substrate concentration and the inhibition by the allosteric activator is the dominant effect in velocity versus substrate curves. These effects are analyzed as a particular case of the concerted allosteric model, assuming that the R state, the conformer displaying the higher affinity for the substrate, is the less catalytic state, thus producing an inverted allosteric response.
650	7	a NATURVETENSKAPx Biologix Biokemi och molekylärbiologi0 (SwePub)106022 hsv//swe
650	7	a NATURAL SCIENCESx Biological Sciencesx Biochemistry and Molecular Biology0 (SwePub)106022 hsv//eng
700	1	a Montero-Morán, Gabriela M4 aut
700	1	a Lara-González, Samuel4 aut
700	1	a Calcagno, Mario L4 aut
710	2	a Laboratorio de Fisicoquímica e Ingeniería de Proteínas, Departamento de Bioquímica, Facultad de Medicina, Universidad Nacional Autónoma de México (UNAM), P.O. Box 70-159, Mexico City, D.F, 04510, Mexico4 org
773	0	t Archives of Biochemistry and Biophysicsd : Elsevier BVg 421:1, s. 77-84q 421:1<77-84x 0003-9861x 1096-0384
856	4 8	u https://urn.kb.se/resolve?urn=urn:nbn:se:umu:diva-156785
856	4 8	u https://doi.org/10.1016/j.abb.2003.09.041

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Av författaren/redakt...: Cisneros, David ...; Montero-Morán, G ...; Lara-González, S ...; Calcagno, Mario ...

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