Pyridoxal phosphate binding sites are similar in human heme-dependent and yeast heme-independent cystathionine beta-synthases. Evidence from 31P NMR and pulsed EPR spectroscopy that heme and PLP cofactors are not proximal in the human enzyme.

Pyridoxal phosphate binding sites are similar in human heme-dependent and yeast heme-independent cystathionine beta-synthases. Evidence from 31P NMR and pulsed EPR spectroscopy that heme and PLP cofactors are not proximal in the human enzyme.

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http://www.wikidata.org/entity/Q43560152
Stopped-flow kinetic analysis of the reaction catalyzed by the full-length yeast cystathionine beta-synthase.Vascular complications of cystathionine β-synthase deficiency: future directions for homocysteine-to-hydrogen sulfide researchReversible heme-dependent regulation of human cystathionine β-synthase by a flavoprotein oxidoreductase.Increased transsulfuration mediates longevity and dietary restriction in Drosophila.PLP-dependent H(2)S biogenesis.Kinetics of Nitrite Reduction and Peroxynitrite Formation by Ferrous Heme in Human Cystathionine β-Synthase.Properties of an unusual heme cofactor in PLP-dependent cystathionine beta-synthase.Kinetics of reversible reductive carbonylation of heme in human cystathionine β-synthase.Methoxistasis: integrating the roles of homocysteine and folic acid in cardiovascular pathobiology.Heme regulation of human cystathionine beta-synthase activity: insights from fluorescence and Raman spectroscopy.Modulation of the heme electronic structure and cystathionine beta-synthase activity by second coordination sphere ligands: The role of heme ligand switching in redox regulation.A small-scale concept-based laboratory component: the best of both worlds.Catalytic promiscuity and heme-dependent redox regulation of H2S synthesis.Chemical Biology of H2S Signaling through Persulfidation.Identification and functional analyses of CBS alleles in Spanish and Argentinian homocystinuric patients.
P2860

Pyridoxal phosphate binding sites are similar in human heme-dependent and yeast heme-independent cystathionine beta-synthases. Evidence from 31P NMR and pulsed EPR spectroscopy that heme and PLP cofactors are not proximal in the human enzyme.

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http://www.wikidata.org/entity/Q43560152
description
2001 nî lūn-bûn
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2001年の論文
@ja
2001年学术文章
@wuu
2001年学术文章
@zh-cn
2001年学术文章
@zh-hans
2001年学术文章
@zh-my
2001年学术文章
@zh-sg
2001年學術文章
@yue
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name
Pyridoxal phosphate binding si ...... proximal in the human enzyme.
@en
Pyridoxal phosphate binding si ...... proximal in the human enzyme.
@nl
type
label
Pyridoxal phosphate binding si ...... proximal in the human enzyme.
@en
Pyridoxal phosphate binding si ...... proximal in the human enzyme.
@nl
prefLabel
Pyridoxal phosphate binding si ...... proximal in the human enzyme.
@en
Pyridoxal phosphate binding si ...... proximal in the human enzyme.
@nl
P1433
P1476
P2093
P2860
P304
P31
P356
P407
P433
P478
P50
P577
P698
P356
P1433
P1476
Pyridoxal phosphate binding si ...... proximal in the human enzyme.
@en
P2093
P2860
P304
P31
P356
P407
P433
P478
P50
P577
P698