Heme biosynthesis in mammalian systems: evidence of a Schiff base linkage between the pyridoxal 5'-phosphate cofactor and a lysine residue in 5-aminolevulinate synthase.

Heme biosynthesis in mammalian systems: evidence of a Schiff base linkage between the pyridoxal 5'-phosphate cofactor and a lysine residue in 5-aminolevulinate synthase.

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http://www.wikidata.org/entity/Q36277762
Circular permutation of 5-aminolevulinate synthase. Mapping the polypeptide chain to its functionCrystal structure of 5-aminolevulinate synthase, the first enzyme of heme biosynthesis, and its link to XLSA in humans.5-aminolevulinate synthase: catalysis of the first step of heme biosynthesisUnstable reaction intermediates and hysteresis during the catalytic cycle of 5-aminolevulinate synthase: implications from using pseudo and alternate substrates and a promiscuous enzyme variant.Functional asymmetry for the active sites of linked 5-aminolevulinate synthase and 8-amino-7-oxononanoate synthase.Expression of murine 5-aminolevulinate synthase variants causes protoporphyrin IX accumulation and light-induced mammalian cell deathCatalytically active alkaline molten globular enzyme: Effect of pH and temperature on the structural integrity of 5-aminolevulinate synthaseRegulation of 5-aminolevulinic acid synthesis in Rhodobacter sphaeroides 2.4.1: the genetic basis of mutant H-5 auxotrophy.Murine erythroid 5-aminolevulinate synthase: Adenosyl-binding site Lys221 modulates substrate binding and catalysisX-linked sideroblastic anemia due to carboxyl-terminal ALAS2 mutations that cause loss of binding to the β-subunit of succinyl-CoA synthetase (SUCLA2).Aminolevulinate synthase: lysine 313 is not essential for binding the pyridoxal phosphate cofactor but is essential for catalysisTransient state kinetic investigation of 5-aminolevulinate synthase reaction mechanism.Heme biosynthesis and its regulation: towards understanding and improvement of heme biosynthesis in filamentous fungiA three enzyme pathway for 2-amino-3-hydroxycyclopent-2-enone formation and incorporation in natural product biosynthesis.Conversion of 5-aminolevulinate synthase into a more active enzyme by linking the two subunits: spectroscopic and kinetic properties.Circular permutation of 5-aminolevulinate synthase: effect on folding, conformational stability, and structure.Lysine 238 is an essential residue for alpha,beta-elimination catalyzed by Treponema denticola cystalysin.
P2860

Heme biosynthesis in mammalian systems: evidence of a Schiff base linkage between the pyridoxal 5'-phosphate cofactor and a lysine residue in 5-aminolevulinate synthase.

Item
http://www.wikidata.org/entity/Q36277762
description
1993 nî lūn-bûn
@nan
1993年の論文
@ja
1993年学术文章
@wuu
1993年学术文章
@zh-cn
1993年学术文章
@zh-hans
1993年学术文章
@zh-my
1993年学术文章
@zh-sg
1993年學術文章
@yue
1993年學術文章
@zh
1993年學術文章
@zh-hant
name
Heme biosynthesis in mammalian ...... in 5-aminolevulinate synthase.
@ast
Heme biosynthesis in mammalian ...... in 5-aminolevulinate synthase.
@en
type
label
Heme biosynthesis in mammalian ...... in 5-aminolevulinate synthase.
@ast
Heme biosynthesis in mammalian ...... in 5-aminolevulinate synthase.
@en
prefLabel
Heme biosynthesis in mammalian ...... in 5-aminolevulinate synthase.
@ast
Heme biosynthesis in mammalian ...... in 5-aminolevulinate synthase.
@en
P1433
P1476
P2093
P2860
P304
P31
P356
P433
P478
P577
P5875
P698
P932
P356
P1433
P1476
Heme biosynthesis in mammalian ...... in 5-aminolevulinate synthase.
@en
P2093
P2860
P304
P31
P356
P433
P478
P577
P5875
P698
P932