Comparison Of The Amino Acid Sequence Of L-Mandelate Dehydrogenase From Rhodotorula Graminis With Other L-2-Hydroxyacid Dehydrogenase Enzyme And Its Primary Structure Prediction
A comparison of the primary structure for L-mandelate dehydrogenase (L-MDH) from Rhodotorula graminis with other proteins from the protein databank suggests that there is similarity between this protein and L-2-hydroxyacid dehydrogenase enzymes. R. graminis LMDH exhibits 26–42% identity to L-lact...
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| Main Authors: | , , |
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| Format: | Article |
| Language: | English |
| Published: |
Penerbit UTM Press
2001
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| Subjects: | |
| Online Access: | http://eprints.utm.my/id/eprint/878/1/JT34C4.pdf http://eprints.utm.my/id/eprint/878/ http://www.penerbit.utm.my/onlinejournal/34/C/JT34C4.pdf |
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| Summary: | A comparison of the primary structure for L-mandelate dehydrogenase (L-MDH) from Rhodotorula graminis with other proteins from the protein databank suggests that there is
similarity between this protein and L-2-hydroxyacid dehydrogenase enzymes. R. graminis LMDH exhibits 26–42% identity to L-lactate dehydrogenase from Saccharomyces cerevisiae, L-lactate dehydrogenase from Hansenula anomala, glycolate oxidase from spinach, L-lactate dehydrogenase from Escherichia coli, L-mandelate dehydrogenase from Pseudomonas putida and lactate-2-monooxygenase from Mycobacterium smegmatis. Structurally conserved amino acids are predicted from LMDH sequences corresponding to important regions of the cytochrome and FMN-binding domain defined from the known three-dimensional structure of the L-lactate dehydrogenase from Saccharomyces cerevisiae. |
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