Human liver glutamic gamma-semialdehyde dehydrogen...[Comp Biochem Physiol B. 1992]

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1: Comp Biochem Physiol B. 1992 Aug;102(4):791-93.Links

Human liver glutamic gamma-semialdehyde dehydrogenase: structural relationship to the yeast enzyme.

Hempel J, Eckey R, Berie D, Romovacek H, Agarwal DP, Goedde HW.

Department of Molecular Genetics and Biochemistry, University of Pittsburgh School of Medicine, PA 15261.

The amino acid sequences of nine tryptic peptides (containing altogether 105 amino acids) from human liver glutamic gamma-semialdehyde of dehydrogenase (hitherto designated as ALDH4) were found to correspond, at 33-66% identity, to segments from the yeast 1-proline-5-carboxylate (P5C) dehydrogenase encoded by the PUT2 gene.

PMID: 1395511 [PubMed - indexed for MEDLINE]

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Sequence analysis identifies the proline dehydrogenase and delta 1-pyrroline-5-carboxylate dehydrogenase domains of the multifunctional Escherichia coli PutA protein. [J Mol Biol. 1994]
ReviewRegulation of levels of proline as an osmolyte in plants under water stress. [Plant Cell Physiol. 1997]
Review[Hyperprolinemia type II] [Ryoikibetsu Shokogun Shirizu. 1998]

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Human liver glutamic gamma-semialdehyde dehydrogenase: structural relationship to the yeast enzyme.

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