Abstract
Glutamate 1-semialdehyde aminotransferase (GSA-AT) has been first described in barley. Gough and Kannangara [1] found an enzyme in the chloroplast stromal preparation of greening barley that catalyses the transamination of glutamate 1-semialdehyde (GSA) to δ-aminolevulinate (ALA). This is the final step of the C5 pathway which in three enzymatic reactions converts glutamate into ALA, the precursor for all tetrapyrroles [2, 3]. The primary structure of GSA-AT from barley has been obtained by partial amino acid sequence determination and nucleotide sequencing of a cDNA clone [4]. Subsequently, a number of bacterial and plant genes for GSA-AT have been sequenced [5–11].
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References
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© 1994 Birkhäuser Verlag Basel/Switzerland
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Grimm, B. (1994). Glutamate 1-semialdehyde aminotransferase, a unique enzyme in chlorophyll biosynthesis. In: Marino, G., Sannia, G., Bossa, F. (eds) Biochemistry of Vitamin B6 and PQQ. Advances in Life Sciences. Birkhäuser Basel. https://doi.org/10.1007/978-3-0348-7393-2_16
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DOI: https://doi.org/10.1007/978-3-0348-7393-2_16
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