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You searched for: Subject spectroscopy Remove constraint Subject: spectroscopy Subject pyridoxal phosphate Remove constraint Subject: pyridoxal phosphate Subject term pyridoxal phosphate Remove constraint Subject term: pyridoxal phosphate
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1. Mechanistic enzymology of serine palmitoyltransferase

Author:
Hiroko Ikushiro; Hideyuki Hayashi
Source:
Biochimica et biophysica acta 2011 v.1814 no.11 pp. 1474-1480
ISSN:
1878-1454
Subject:
biosynthesis; pyridoxal phosphate; sphingolipids; spectroscopy; enzymology; serine C-palmitoyltransferase
Abstract:
... Serine palmitoyltransferase, which is one of the α-oxamine synthase family enzymes, catalyzes the condensation reaction of L-serine and palmitoyl-CoA to form 3-ketodihydrosphingosine, the first and rate-determining step of the sphingolipid biosynthesis. As with other α-oxamine synthase family enzymes, the catalytic reaction is composed of multiple elementary steps, and the mechanism to control the ...
DOI:
10.1016/j.bbapap.2011.02.005

2. Properties of an unusual heme cofactor in PLP-dependent cystathionine β-synthase

Author:
Sangita Singh; Peter Madzelan; Ruma Banerjee
Source:
Natural product reports 2007 v.24 no.3 pp. 631-639
ISSN:
1460-4752
Subject:
active sites; crystal structure; cystathionine; heme; heme iron; heme proteins; homocysteine; ligands; oxidation; pyridoxal phosphate; serine; signal transduction; spectroscopy
Abstract:
... Cystathionine β-synthase is a pyridoxal phosphate (PLP)-dependent hemeprotein, which catalyzes the condensation of serine and homocysteine to give cystathionine, the first step in the transsulfuration pathway. The association of heme with this enzyme in some organisms, including humans, is novel since this combination of cofactors has not been seen in any other protein to date. While the role of P ...
DOI:
10.1039/b604182p

3. The biosynthesis of ovothiol A (N1‐methyl‐4‐mercaptohistidine) : Identification of S‐(4′‐l‐histidyl)‐l‐cysteine sulfoxide as an intermediate and the products of the sulfoxide lyase reaction

Author:
Ryan N. Vogt; Hendrik S. C. Spies; Daniel J. Steenkamp
Source:
European journal of biochemistry 2001 v.268 no.20 pp. 5229-5241
ISSN:
0014-2956
Subject:
Crithidia fasciculata; NAD (coenzyme); NADH dehydrogenase; ammonium sulfate; anion exchange chromatography; biosynthesis; cysteine; dithiothreitol; high performance liquid chromatography; histidine; iron; isotope labeling; lactate dehydrogenase; oxygen; pyridoxal phosphate; pyruvic acid; spectral analysis; spectroscopy; sulfur; thiols
Abstract:
... Crude extracts of Crithidia fasciculata catalyse the formation of 4‐mercapto‐l‐histidine, an intermediate in the biosynthesis of ovothiol A (N1‐methyl‐4‐mercaptohistidine), in the presence of histidine, cysteine, Fe2+ and pyridoxal phosphate. This activity was present in a 35–55% ammonium sulfate fraction that was shown to produce a transsulfuration intermediate in the absence of pyr ...
DOI:
10.1046/j.0014-2956.2001.02444.x