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Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)
 

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Proline biosynthesis in Escherichia coli. Purification and characterisation of glutamate-semialdehyde dehydrogenase.

Glutamate-semialdehyde dehydrogenase, catalysing the reduction in vivo of gamma-glutamyl phosphate to glutamate 5-semialdehyde in the pathway of proline biosynthesis in Escherichia coli, has been purified to homogeneity. High initial levels of the enzyme were achieved by using a multicopy ColEl-pro A, B hybrid plasmid. The protein has a molecular weight of 1.89 X 10(5) and consists of four identical subunits of molecular weight 4.7 X 10(4) each. The pH optimum is 7.0 and the protein is stable for at least 10 min between pH 6.0-9.0 and for long periods at pH 7.0 It is rapidly inactivated at temperatures greater than 50 degrees C. The enzyme is very sensitive to inhibition by p-chloro-mercuribenzoate, copper and nickel ions.[1]

References

  1. Proline biosynthesis in Escherichia coli. Purification and characterisation of glutamate-semialdehyde dehydrogenase. Hayzer, D.J., Leisinger, T. Eur. J. Biochem. (1982) [Pubmed]
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