Detalhe da pesquisa
1.
5-Aminolevulinate synthase catalysis: The catcher in heme biosynthesis.
Mol Genet Metab
; 128(3): 178-189, 2019 11.
Artigo
em Inglês
| MEDLINE | ID: mdl-31345668
2.
Ferrochelatase π-helix: Implications from examining the role of the conserved π-helix glutamates in porphyrin metalation and product release.
Arch Biochem Biophys
; 644: 37-46, 2018 04 15.
Artigo
em Inglês
| MEDLINE | ID: mdl-29481781
3.
The Structure of the Complex between Yeast Frataxin and Ferrochelatase: CHARACTERIZATION AND PRE-STEADY STATE REACTION OF FERROUS IRON DELIVERY AND HEME SYNTHESIS.
J Biol Chem
; 291(22): 11887-98, 2016 May 27.
Artigo
em Inglês
| MEDLINE | ID: mdl-27026703
4.
Human Erythroid 5-Aminolevulinate Synthase Mutations Associated with X-Linked Protoporphyria Disrupt the Conformational Equilibrium and Enhance Product Release.
Biochemistry
; 54(36): 5617-31, 2015 Sep 15.
Artigo
em Inglês
| MEDLINE | ID: mdl-26300302
5.
Unstable reaction intermediates and hysteresis during the catalytic cycle of 5-aminolevulinate synthase: implications from using pseudo and alternate substrates and a promiscuous enzyme variant.
J Biol Chem
; 289(33): 22915-22925, 2014 Aug 15.
Artigo
em Inglês
| MEDLINE | ID: mdl-24920668
6.
Catalytically active alkaline molten globular enzyme: Effect of pH and temperature on the structural integrity of 5-aminolevulinate synthase.
Biochim Biophys Acta
; 1844(12): 2145-54, 2014 Dec.
Artigo
em Inglês
| MEDLINE | ID: mdl-25240868
7.
Aminolaevulinic acid synthase of Rhodobacter capsulatus: high-resolution kinetic investigation of the structural basis for substrate binding and catalysis.
Biochem J
; 451(2): 205-16, 2013 Apr 15.
Artigo
em Inglês
| MEDLINE | ID: mdl-23363548
8.
Porphyrin overdrive rewires cancer cell metabolism.
Life Sci Alliance
; 7(7)2024 Jul.
Artigo
em Inglês
| MEDLINE | ID: mdl-38649187
9.
Molecular enzymology of 5-aminolevulinate synthase, the gatekeeper of heme biosynthesis.
Biochim Biophys Acta
; 1814(11): 1467-73, 2011 Nov.
Artigo
em Inglês
| MEDLINE | ID: mdl-21215825
10.
An Extended C-Terminus, the Possible Culprit for Differential Regulation of 5-Aminolevulinate Synthase Isoforms.
Front Mol Biosci
; 9: 920668, 2022.
Artigo
em Inglês
| MEDLINE | ID: mdl-35911972
11.
Serine 254 enhances an induced fit mechanism in murine 5-aminolevulinate synthase.
J Biol Chem
; 285(5): 3351-9, 2010 Jan 29.
Artigo
em Inglês
| MEDLINE | ID: mdl-19917609
12.
Identification and characterization of an inhibitory metal ion-binding site in ferrochelatase.
J Biol Chem
; 285(53): 41836-42, 2010 Dec 31.
Artigo
em Inglês
| MEDLINE | ID: mdl-20966079
13.
Targeting the active site gate to yield hyperactive variants of 5-aminolevulinate synthase.
J Biol Chem
; 285(18): 13704-11, 2010 Apr 30.
Artigo
em Inglês
| MEDLINE | ID: mdl-20194506
14.
Functional asymmetry for the active sites of linked 5-aminolevulinate synthase and 8-amino-7-oxononanoate synthase.
Arch Biochem Biophys
; 511(1-2): 107-17, 2011 Jul.
Artigo
em Inglês
| MEDLINE | ID: mdl-21600186
15.
Correction: Porphyrin overdrive rewires cancer cell metabolism.
Life Sci Alliance
; 7(8)2024 Aug.
Artigo
em Inglês
| MEDLINE | ID: mdl-38803226
16.
Expression of murine 5-aminolevulinate synthase variants causes protoporphyrin IX accumulation and light-induced mammalian cell death.
PLoS One
; 9(4): e93078, 2014.
Artigo
em Inglês
| MEDLINE | ID: mdl-24718052
17.
FERROCHELATASE: THE CONVERGENCE OF THE PORPHYRIN BIOSYNTHESIS AND IRON TRANSPORT PATHWAYS.
J Porphyr Phthalocyanines
; 15(5-6): 350-356, 2011.
Artigo
em Inglês
| MEDLINE | ID: mdl-21852895
18.
Arg-85 and Thr-430 in murine 5-aminolevulinate synthase coordinate acyl-CoA-binding and contribute to substrate specificity.
Protein Sci
; 18(9): 1847-59, 2009 Sep.
Artigo
em Inglês
| MEDLINE | ID: mdl-19562746
19.
Metal ion substrate inhibition of ferrochelatase.
J Biol Chem
; 283(35): 23685-91, 2008 Aug 29.
Artigo
em Inglês
| MEDLINE | ID: mdl-18593702
20.
Transient kinetic studies support refinements to the chemical and kinetic mechanisms of aminolevulinate synthase.
J Biol Chem
; 282(32): 23025-35, 2007 Aug 10.
Artigo
em Inglês
| MEDLINE | ID: mdl-17485466