Detalles de la búsqueda
1.
Persulfide Transfer to SufE Activates the Half-Sites Reactivity of the E. coli Cysteine Desulfurase SufS.
Biochemistry
; 63(12): 1569-1577, 2024 Jun 18.
Artículo
en Inglés
| MEDLINE | ID: mdl-38813769
2.
In Vitro and In Silico Explorations of the Protein Conformational Changes of Corynebacterium glutamicum MshA, a Model Retaining GT-B Glycosyltransferase.
Biochemistry
; 63(7): 939-951, 2024 Apr 02.
Artículo
en Inglés
| MEDLINE | ID: mdl-38507812
3.
The ß-latch structural element of the SufS cysteine desulfurase mediates active site accessibility and SufE transpersulfurase positioning.
J Biol Chem
; 299(3): 102966, 2023 03.
Artículo
en Inglés
| MEDLINE | ID: mdl-36736428
4.
HDX-MS Reveals Substrate-Dependent, Localized EX1 Conformational Dynamics in the Retaining GT-B Glycosyltransferase, MshA.
Biochemistry
; 62(17): 2645-2657, 2023 09 05.
Artículo
en Inglés
| MEDLINE | ID: mdl-37589157
5.
Direct observation of intermediates in the SufS cysteine desulfurase reaction reveals functional roles of conserved active-site residues.
J Biol Chem
; 294(33): 12444-12458, 2019 08 16.
Artículo
en Inglés
| MEDLINE | ID: mdl-31248989
6.
Biochemical characterization of 2-phosphinomethylmalate synthase from Streptomyces hygroscopicus: A member of the DRE-TIM metallolyase superfamily.
Arch Biochem Biophys
; 691: 108489, 2020 09 30.
Artículo
en Inglés
| MEDLINE | ID: mdl-32697946
7.
Structural Evidence for Dimer-Interface-Driven Regulation of the Type II Cysteine Desulfurase, SufS.
Biochemistry
; 58(6): 687-696, 2019 02 12.
Artículo
en Inglés
| MEDLINE | ID: mdl-30571100
8.
Distinct mechanisms of substrate selectivity in the DRE-TIM metallolyase superfamily: A role for the LeuA dimer regulatory domain.
Arch Biochem Biophys
; 664: 1-8, 2019 03 30.
Artículo
en Inglés
| MEDLINE | ID: mdl-30668939
9.
Changes in Protein Dynamics in Escherichia coli SufS Reveal a Possible Conserved Regulatory Mechanism in Type II Cysteine Desulfurase Systems.
Biochemistry
; 57(35): 5210-5217, 2018 09 04.
Artículo
en Inglés
| MEDLINE | ID: mdl-29589903
10.
Improving Functional Annotation in the DRE-TIM Metallolyase Superfamily through Identification of Active Site Fingerprints.
Biochemistry
; 55(12): 1863-72, 2016 Mar 29.
Artículo
en Inglés
| MEDLINE | ID: mdl-26935545
11.
SufE D74R Substitution Alters Active Site Loop Dynamics To Further Enhance SufE Interaction with the SufS Cysteine Desulfurase.
Biochemistry
; 54(31): 4824-33, 2015 Aug 11.
Artículo
en Inglés
| MEDLINE | ID: mdl-26171726
12.
An evolutionarily conserved alternate metal ligand is important for activity in α-isopropylmalate synthase from Mycobacterium tuberculosis.
Biochim Biophys Acta
; 1844(10): 1784-9, 2014 Oct.
Artículo
en Inglés
| MEDLINE | ID: mdl-25064783
13.
Evolutionarily distinct versions of the multidomain enzyme α-isopropylmalate synthase share discrete mechanisms of V-type allosteric regulation.
Biochemistry
; 53(29): 4847-56, 2014 Jul 29.
Artículo
en Inglés
| MEDLINE | ID: mdl-24991690
14.
Mechanistic and bioinformatic investigation of a conserved active site helix in α-isopropylmalate synthase from Mycobacterium tuberculosis, a member of the DRE-TIM metallolyase superfamily.
Biochemistry
; 53(18): 2915-25, 2014 May 13.
Artículo
en Inglés
| MEDLINE | ID: mdl-24720347
15.
Biochemical characterization of the retaining glycosyltransferase glucosyl-3-phosphoglycerate synthase from Mycobacterium tuberculosis.
Arch Biochem Biophys
; 564: 120-7, 2014 Dec 15.
Artículo
en Inglés
| MEDLINE | ID: mdl-25317963
16.
The structure of the SufS-SufE complex reveals interactions driving protected persulfide transfer in iron-sulfur cluster biogenesis.
bioRxiv
; 2024 May 24.
Artículo
en Inglés
| MEDLINE | ID: mdl-38826363
17.
V-type allosteric inhibition is described by a shift in the rate-determining step for α-isopropylmalate synthase from Mycobacterium tuberculosis.
Biochemistry
; 52(39): 6737-9, 2013 Oct 01.
Artículo
en Inglés
| MEDLINE | ID: mdl-24033269
18.
Identification and analysis of small molecule inhibitors of FosB from Staphylococcus aureus.
RSC Med Chem
; 14(5): 947-956, 2023 May 25.
Artículo
en Inglés
| MEDLINE | ID: mdl-37252104
19.
The slow-onset nature of allosteric inhibition in α-isopropylmalate synthase from Mycobacterium tuberculosis is mediated by a flexible loop.
Biochemistry
; 51(24): 4773-5, 2012 Jun 19.
Artículo
en Inglés
| MEDLINE | ID: mdl-22662746
20.
Structural and functional characterization of α-isopropylmalate synthase and citramalate synthase, members of the LeuA dimer superfamily.
Arch Biochem Biophys
; 519(2): 202-9, 2012 Mar 15.
Artículo
en Inglés
| MEDLINE | ID: mdl-22033339