Enzyme - EC
1.2.1.38 - N-acetyl-gamma-glutamyl-phosphate reductase |
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The tridimensional structure
of this enzyme has not been resolved yet. |
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EC |
1.2.1.38 |
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Official
Name |
N-acetyl-gamma-glutamyl-phosphate reductase |
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Alternative
name(s) |
N-acetyl-glutamate semialdehyde dehydrogenase NAGSA dehydrogenase |
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Class |
1.Oxidoreductases 2.Acting on the aldehyde or oxo group of donors 1.With NAD+ or NADP+ as acceptor |
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Reaction
catalysed |
N-acetyl-L-glutamate
5-semialdehyde + NADP+ + PN-acetyl-5-glutamyl-P
+ NADPH |
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Substrates |
N-acetyl-L-glutamate 5-semialdehyde NADP+ Orthophosphate |
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Products |
N-acetyl-5-glutamyl-P NADPH |
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Metabolic Pathways |
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Other
comments |
N-acetyl-gamma-glutamyl-phosphate reductase is the enzyme that catalyzes the third step in the biosynthesis of arginine from glutamate, the NADP-dependent reduction of N-acetyl-5-glutamyl phosphate into N-acetylglutamate 5-semialdehyde. In bacteria it is a monofunctional protein of 35 to 38 Kd (gene argC) while in fungi it is part of a bifunctional mitochondrial enzyme (gene ARG5,6, arg11 or arg-6) which contains a N-terminal acetylglutamate kinase (EC 2.7.2.8) domain and a C-terminal AGPR domain. |
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In the Escherichia coli enzyme, a cysteine has been shown to be implicated in
the catalytic activity, the region around this residue is well conserved and
can be used as a signature pattern. |
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