Glutamate-5-semialdehyde dehydrogenase

Chemical Enzyme From Wikipedia, the free encyclopedia

In enzymology, glutamate-5-semialdehyde dehydrogenase (EC 1.2.1.41) is an enzyme that catalyzes the chemical reaction

 
 
Pi
H+
Reversible left-right reaction arrow with minor forward substrate(s) from top left, minor forward product(s) to top right, minor reverse substrate(s) from bottom right and minor reverse product(s) to bottom left
Pi
H+
 
2D representation of the chemical structure of Q27102623.
L-γ-glutamyl phosphate
 

The three substrates of this enzyme are L-glutamate-5-semialdehyde, oxidised nicotinamide adenine dinucleotide phosphate (NADP+) and phosphate (Pi). Its products are L-γ-glutamyl phosphate, reduced NADPH, and a proton.[1][2]

This enzyme belongs to the family of oxidoreductases, specifically those acting on the aldehyde or oxo group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is L-glutamate-5-semialdehyde:NADP+ 5-oxidoreductase (phosphorylating). Other names in common use include beta-glutamylphosphate reductase, gamma-glutamyl phosphate reductase, beta-glutamylphosphate reductase, glutamate semialdehyde dehydrogenase, and glutamate-gamma-semialdehyde dehydrogenase. This enzyme participates in urea cycle and metabolism of amino groups.

Structural studies

As of late 2007, 3 structures have been solved for this class of enzymes, with PDB accession codes PDB: 1O20, PDB: 1VLU, and PDB: 2H5G.

References

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