| EC |
1.2.1.70 |
| Accepted name: |
glutamyl-tRNA reductase |
| Reaction: |
L-glutamate 1-semialdehyde + NADP+ + tRNAGlu = L-glutamyl-tRNAGlu + NADPH + H+ |
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For diagram of the early stages of porphyrin biosynthesis, click here |
| Systematic name: |
L-glutamate-semialdehyde:NADP+ oxidoreductase (L-glutamyl-tRNAGlu-forming) |
| Comments: |
This enzyme forms part of the pathway for the biosynthesis of 5-aminolevulinate from glutamate, known as the C5 pathway. The route shown in the diagram is used in most eubacteria, and in all archaebacteria, algae and plants. However, in the α-proteobacteria, EC 2.3.1.37, 5-aminolevulinate synthase, is used in an alternative route to produce the product 5-aminolevulinate from succinyl-CoA and glycine. This route is found in the mitochondria of fungi and animals, organelles that are considered to be derived from an endosymbiotic α-proteobacterium. Although higher plants do not possess EC 2.3.1.37, the protistan Euglena gracilis possesses both the C5 pathway and EC 2.3.1.37. |
| Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 119940-26-0 |
| References: |
| 1. |
von Wettstein, D., Gough, S. and Kannangara, C.G. Chlorophyll biosynthesis. Plant Cell 7 (1995) 1039–1057. [DOI] [PMID: 12242396] |
| 2. |
Pontoppidan, B. and Kannangara, C.G. Purification and partial characterisation of barley glutamyl-tRNAGlu reductase, the enzyme that directs glutamate to chlorophyll biosynthesis. Eur. J. Biochem. 225 (1994) 529–537. [DOI] [PMID: 7957167] |
| 3. |
Schauer, S., Chaturvedi, S., Randau, L., Moser, J., Kitabatake, M., Lorenz, S., Verkamp, E., Schubert, W.D., Nakayashiki, T., Murai, M., Wall, K., Thomann, H.-U., Heinz, D.W., Inokuchi, H, Söll, D. and Jahn, D. Escherichia coli glutamyl-tRNA reductase. Trapping the thioester intermediate. J. Biol. Chem. 277 (2002) 48657–48663. [DOI] [PMID: 12370189] |
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| [EC 1.2.1.70 created 2004] |
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| EC |
5.4.3.8 |
| Accepted name: |
glutamate-1-semialdehyde 2,1-aminomutase |
| Reaction: |
L-glutamate 1-semialdehyde = 5-aminolevulinate |
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For diagram of the early stages of porphyrin biosynthesis, click here and for mechanism of reaction, click here |
| Glossary: |
L-glutamate 1-semialdehyde = (S)-4-amino-5-oxopentanoate |
| Other name(s): |
glutamate-1-semialdehyde aminotransferase |
| Systematic name: |
(S)-4-amino-5-oxopentanoate 4,5-aminomutase |
| Comments: |
Requires pyridoxal phosphate. |
| Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 68518-07-0 |
| References: |
| 1. |
Gough, S.P. and Kannangara, C.G. Biosynthesis of δ-aminolevulinate in greening barley leaves: glutamate 1-semialdehyde aminotransferase. Carlsberg Res. Commun. 43 (1978) 185–194. |
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| [EC 5.4.3.8 created 1983] |
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