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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| Format: | Article |
| Language: | English |
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Penerbit UTM Press
2001
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| Online Access: | http://eprints.utm.my/878/ http://eprints.utm.my/878/1/JT34C4.pdf |
| _version_ | 1848890017973272576 |
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| author | Md. Illias, Rosli Reid, Graeme A. A. Wahab, Nadzarah |
| author_facet | Md. Illias, Rosli Reid, Graeme A. A. Wahab, Nadzarah |
| author_sort | Md. Illias, Rosli |
| building | UTeM Institutional Repository |
| collection | Online Access |
| description | 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. |
| first_indexed | 2025-11-15T20:35:23Z |
| format | Article |
| id | utm-878 |
| institution | Universiti Teknologi Malaysia |
| institution_category | Local University |
| language | English |
| last_indexed | 2025-11-15T20:35:23Z |
| publishDate | 2001 |
| publisher | Penerbit UTM Press |
| recordtype | eprints |
| repository_type | Digital Repository |
| spelling | utm-8782017-11-01T04:17:50Z http://eprints.utm.my/878/ 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 Md. Illias, Rosli Reid, Graeme A. A. Wahab, Nadzarah TP Chemical technology 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. Penerbit UTM Press 2001-06 Article PeerReviewed application/pdf en http://eprints.utm.my/878/1/JT34C4.pdf Md. Illias, Rosli and Reid, Graeme A. and A. Wahab, Nadzarah (2001) 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. Jurnal Teknologi C (34C). pp. 25-34. ISSN 0127-9696 http://www.penerbit.utm.my/onlinejournal/34/C/JT34C4.pdf |
| spellingShingle | TP Chemical technology Md. Illias, Rosli Reid, Graeme A. A. Wahab, Nadzarah 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 |
| title | 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 |
| title_full | 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 |
| title_fullStr | 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 |
| title_full_unstemmed | 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 |
| title_short | 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 |
| title_sort | 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 |
| topic | TP Chemical technology |
| url | http://eprints.utm.my/878/ http://eprints.utm.my/878/ http://eprints.utm.my/878/1/JT34C4.pdf |