EXCHANGE OF THE VALINE-2-H IN THE BIOSYNTHESIS OF L-DELTA-(ALPHA-AMINOADIPOYL)-L-CYSTEINYL-D-VALINE
Incubation of [2-2H]-valine with purified ACV synthetase from both Cephalosporium acremonium and Streptomyces clavuligerus produced L-δ-(α-aminoadipoyl)-L-cysteinyl-D-valine (ACV), determined by the essentially complete (>95%) loss of deuterium from the α position of the incorporated valine....
| Main Authors: | , , , , , |
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| 格式: | Journal article |
| 語言: | English |
| 出版: |
1993
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| _version_ | 1826276716157337600 |
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| author | Baldwin, J Byford, M Field, R Shiau, C Sobey, W Schofield, C |
| author_facet | Baldwin, J Byford, M Field, R Shiau, C Sobey, W Schofield, C |
| author_sort | Baldwin, J |
| collection | OXFORD |
| description | Incubation of [2-2H]-valine with purified ACV synthetase from both Cephalosporium acremonium and Streptomyces clavuligerus produced L-δ-(α-aminoadipoyl)-L-cysteinyl-D-valine (ACV), determined by the essentially complete (>95%) loss of deuterium from the α position of the incorporated valine. Incubations with deuterium oxide/water as solvent produced ACV with significant incorporation of deuterium into the valinyl residue. These observations confirm the prior proposal that a single multifunctional enzyme is responsible for both the formation of the peptide bonds of ACV and the epimerisation of the valinyl residue. © 1993. |
| first_indexed | 2024-03-06T23:18:04Z |
| format | Journal article |
| id | oxford-uuid:67ceaeb4-594a-4668-9991-a033cbf68460 |
| institution | University of Oxford |
| language | English |
| last_indexed | 2024-03-06T23:18:04Z |
| publishDate | 1993 |
| record_format | dspace |
| spelling | oxford-uuid:67ceaeb4-594a-4668-9991-a033cbf684602022-03-26T18:40:45ZEXCHANGE OF THE VALINE-2-H IN THE BIOSYNTHESIS OF L-DELTA-(ALPHA-AMINOADIPOYL)-L-CYSTEINYL-D-VALINEJournal articlehttp://purl.org/coar/resource_type/c_dcae04bcuuid:67ceaeb4-594a-4668-9991-a033cbf68460EnglishSymplectic Elements at Oxford1993Baldwin, JByford, MField, RShiau, CSobey, WSchofield, CIncubation of [2-2H]-valine with purified ACV synthetase from both Cephalosporium acremonium and Streptomyces clavuligerus produced L-δ-(α-aminoadipoyl)-L-cysteinyl-D-valine (ACV), determined by the essentially complete (>95%) loss of deuterium from the α position of the incorporated valine. Incubations with deuterium oxide/water as solvent produced ACV with significant incorporation of deuterium into the valinyl residue. These observations confirm the prior proposal that a single multifunctional enzyme is responsible for both the formation of the peptide bonds of ACV and the epimerisation of the valinyl residue. © 1993. |
| spellingShingle | Baldwin, J Byford, M Field, R Shiau, C Sobey, W Schofield, C EXCHANGE OF THE VALINE-2-H IN THE BIOSYNTHESIS OF L-DELTA-(ALPHA-AMINOADIPOYL)-L-CYSTEINYL-D-VALINE |
| title | EXCHANGE OF THE VALINE-2-H IN THE BIOSYNTHESIS OF L-DELTA-(ALPHA-AMINOADIPOYL)-L-CYSTEINYL-D-VALINE |
| title_full | EXCHANGE OF THE VALINE-2-H IN THE BIOSYNTHESIS OF L-DELTA-(ALPHA-AMINOADIPOYL)-L-CYSTEINYL-D-VALINE |
| title_fullStr | EXCHANGE OF THE VALINE-2-H IN THE BIOSYNTHESIS OF L-DELTA-(ALPHA-AMINOADIPOYL)-L-CYSTEINYL-D-VALINE |
| title_full_unstemmed | EXCHANGE OF THE VALINE-2-H IN THE BIOSYNTHESIS OF L-DELTA-(ALPHA-AMINOADIPOYL)-L-CYSTEINYL-D-VALINE |
| title_short | EXCHANGE OF THE VALINE-2-H IN THE BIOSYNTHESIS OF L-DELTA-(ALPHA-AMINOADIPOYL)-L-CYSTEINYL-D-VALINE |
| title_sort | exchange of the valine 2 h in the biosynthesis of l delta alpha aminoadipoyl l cysteinyl d valine |
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