New Aspects of the Intermediates, Catalytic Components and the Regulation of the C5 -Pathway to Chlorophyll

1992 ◽  
pp. 175-181 ◽  
Author(s):  
D. Dörnemann
Keyword(s):  
C5 Pathway

13C-NMR evidence of bacteriochlorophyll a formation by the C5 pathway in Chromatium

1986 ◽  
Vol 246 (1) ◽  
pp. 192-198 ◽  
Author(s):  
Tamiko Oh-hama ◽  
Haruo Seto ◽  
Shigetoh Miyachi
Keyword(s):  
13C Nmr ◽  
Bacteriochlorophyll A ◽  
C5 Pathway

scholarly journals Challenges and opportunities of bioprocessing 5-aminolevulinic acid using genetic and metabolic engineering: a critical review

2021 ◽  
Vol 8 (1) ◽  
Author(s):  
Ying-Chen Yi ◽  
I-Tai Shih ◽  
Tzu-Hsuan Yu ◽  
Yen-Ju Lee ◽  
I-Son Ng
Keyword(s):  
Metabolic Engineering ◽  
Pyridoxal Phosphate ◽  
Aminolevulinic Acid ◽  
Tca Cycle ◽  
Industrial Applications ◽  
Trna Synthetase ◽  
The Us ◽  
Challenges And Opportunities ◽  
One Step ◽  
C5 Pathway

Abstract5-Aminolevulinic acid (5-ALA), a non-proteinogenic five-carbon amino acid, has received intensive attentions in medicine due to its approval by the US Food and Drug Administration (FDA) for cancer diagnosis and treatment as photodynamic therapy. As chemical synthesis of 5-ALA performed low yield, complicated processes, and high cost, biosynthesis of 5-ALA via C4 (also called Shemin pathway) and C5 pathway related to heme biosynthesis in microorganism equipped more advantages. In C4 pathway, 5-ALA is derived from condensation of succinyl-CoA and glycine by 5-aminolevulic acid synthase (ALAS) with pyridoxal phosphate (PLP) as co-factor in one-step biotransformation. The C5 pathway involves three enzymes comprising glutamyl-tRNA synthetase (GltX), glutamyl-tRNA reductase (HemA), and glutamate-1-semialdehyde aminotransferase (HemL) from α-ketoglutarate in TCA cycle to 5-ALA and heme. In this review, we describe the recent results of 5-ALA production from different genes and microorganisms via genetic and metabolic engineering approaches. The regulation of different chassis is fine-tuned by applying synthetic biology and boosts 5-ALA production eventually. The purification process, challenges, and opportunities of 5-ALA for industrial applications are also summarized.

scholarly journals Glutamate-1-semialdehyde aminotransferase from Sulfolobus solfataricus*

1996 ◽  
Vol 320 (2) ◽  
pp. 541-545 ◽  
Author(s):  
Gianna PALMIERI ◽  
Michela DI PALO ◽  
Andrea SCALONI ◽  
Stefania ORRÙ ◽  
Gennaro MARINO ◽  
...  
Keyword(s):  
Absorption Spectrum ◽  
Sulfolobus Solfataricus ◽  
Active Form ◽  
Thermophilic Bacterium ◽  
Aminotransferase Activity ◽  
Terminal Amino Acid ◽  
Significant Similarity ◽  
Terminal Amino ◽  
C5 Pathway ◽  
Terminal Amino Acid Sequence

Glutamate-1-semialdehyde aminotransferase (GSA-AT) from the extremely thermophilic bacterium Sulfolobus solfataricus has been purified to homogeneity and characterized. GSA-AT is the last enzyme in the C5 pathway for the conversion of glutamate into the tetrapyrrole precursor Δ-aminolaevulinate (ALA) in plants, algae and several bacteria. The active form of GSA-AT from S. solfataricus seems to be a homodimer with a molecular mass of 87 kDa. The absorption spectrum of the purified aminotransferase is indicative of the presence of pyridoxamine 5´-phosphate (PMP) cofactor, and the catalytic activity of the enzyme is further stimulated by addition of PMP. 3-Amino-2,3-dihydrobenzoic acid is an inhibitor of the aminotransferase activity. The N-terminal amino acid sequence of GSA-AT from S. solfataricus was found to share significant similarity with the eukaryotic and eubacterial enzymes. Evidence is provided that ALA synthesis in S. solfataricus follows the C5 pathway characteristic of plants, algae, cyanobacteria and many other bacteria.

Charging of Both, Plastidal tRNAgln and tRNAglu with Glutamate and Subsequent Amidation of the Misacylated tRNAgln by a Glutamyl-tRNA Amidotransferase in the Unicellular Green Alga Scenedesmus obliquus, Mutant C-2A'

1995 ◽  
Vol 50 (11-12) ◽  
pp. 789-795 ◽  
Author(s):  
U. C Vothknecht ◽  
D Dörnemann
Keyword(s):  
Green Alga ◽  
Cyanogen Bromide ◽  
Protein Biosynthesis ◽  
Scenedesmus Obliquus ◽  
Trna Synthetase ◽  
Higher Plant ◽  
Gram Positive Bacteria ◽  
Unicellular Green Alga ◽  
C5 Pathway ◽  
Sulfur Modification

Abstract , 1995 C5-Pathway, Glutamyl-tRNAglu-Synthetase (E.C.6.1.1.17), Misacylation of tR N A glu, Amidotransferase, Scenedesmus obliquus In a previous paper we described the purification of a glutamyl-tRNA synthetase from the unicellular green alga Scenedesmus obliquus, m utant C-2A'. We now dem onstrate that, firstly, this enzyme is capable of mischarging plastidal tR N A gln from barley with glutamate, as well as it regularly charges the plastidal tR N A glu from Scenedesmus. Secondly, we show that the mischarged glutamyl-tRNAgln is subsequently am idated by a glutamyl-tRNA am idotransfer­ ase to form the glutaminyl-tRNAglri required for plastidal protein biosynthesis. This phenom ­ enon could already be dem onstrated for higher plant chloroplasts, mitochondria, cyanobact­ eria and gram-positive bacteria, as far as investigated. As recently shown the applied glutamyl-tRNA synthetase from Scenedesmus is a plastidal enzyme. In this paper we prove by treatm ent with m onobromobim ane and cyanogen bromide that the "regular" substrate of the enzyme, tR N A glu from Scenedesmus, is a plastidal tRNA with the plastid-specific sulfur modification in the anticodon. In the case of cyanogen bromide treatm ent, a total inactivation of the tRNA was achieved, revealing the presence of a sulfur modification in the plastid-tRNA glu anticodon.

Inhibition of Bacteriochlorophyll Biosynthesis by Gabaculin (3-Amino, 2,3-dihydrobenzoic Acid) and Presence of an Enzyme of the C5-Pathway of δ-Aminolevulinate Synthesis in Chloroflexus aurantiacus

1989 ◽  
Vol 44 (1-2) ◽  
pp. 77-80 ◽  
Author(s):  
Monika Kern ◽  
Jobst-Heinrich Klemme
Keyword(s):  
Chloroflexus Aurantiacus ◽  
Bacteriochlorophyll C ◽  
Cell Extracts ◽  
Highly Sensitive ◽  
Key Enzyme ◽  
C5 Pathway ◽  
Bacteriochlorophyll Biosynthesis

Abstract Biosynthesis of bacteriochlorophyll c and a in the thermophilic phototrophic prokaryote. Chloroflexus aurantiacus Ok-70-fl, was strongly inhibited by the antibiotic gabaculin (3-amino 2,3- dihydrobenzoic acid), an inhibitor of the glutamate-C5-pathway of ö-aminolevulinate (ALA) synthesis. The key enzyme of the Shemin-pathway of ALA formation, ALA synthase (EC 2.3.1.37), was not detected in cell extracts of Chi. aurantiacus. However, the extracts catalyzed ALA formation from glutamate 1-semialdehyde, a reaction being highly sensitive to gabaculin.

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