Stereospecificity of sodium borohydride reduction of tyrosine decarboxylase from Streptococcus faecalis
Sodium boro[3H]hydride reduction of tyrosine decarboxylase from Streptococcus faecalis followed by complete hydrolysis of the enzyme produces epsilon-[3H]pyridoxyllysine. Degradation of this material to [4'-3H]pyridoxamine and stereochemical analysis with apoaspartate aminotransferase shows that the re side at C-4' of the cofactor is exposed to solvent at pH 5.5 and 7.0. After binding of L-tyrosine at pH 5.5 or tyramine at pH 7.0 to the holoenzyme, sodium boro[3H]hydride reduction proceeds from the si face at C-4' of the substrate . cofactor complex. This indicates one of two conformational changes occurs upon binding of substrate; either rotation about the C-4 to C-4' bond in the cofactor or rotation about the axis through the C-5 and C-5' bond.
| Medienart: |
Artikel |
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| Erscheinungsjahr: |
1979 |
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| Erschienen: |
1979 |
| Enthalten in: |
Zur Gesamtaufnahme - volume:254 |
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| Enthalten in: |
The Journal of biological chemistry - 254(1979), 12 vom: 25. Juni, Seite 5053-7 |
| Sprache: |
Englisch |
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| Beteiligte Personen: |
Vederas, J C [VerfasserIn] |
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| Themen: |
3THM379K8A |
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| Anmerkungen: |
Date Completed 16.08.1979 Date Revised 10.02.2021 published: Print Citation Status MEDLINE |
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| Förderinstitution / Projekttitel: |
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| PPN (Katalog-ID): |
NLM000375519 |
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| 100 | 1 | |a Vederas, J C |e verfasserin |4 aut | |
| 245 | 1 | 0 | |a Stereospecificity of sodium borohydride reduction of tyrosine decarboxylase from Streptococcus faecalis |
| 264 | 1 | |c 1979 | |
| 336 | |a Text |b txt |2 rdacontent | ||
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| 500 | |a Date Completed 16.08.1979 | ||
| 500 | |a Date Revised 10.02.2021 | ||
| 500 | |a published: Print | ||
| 500 | |a Citation Status MEDLINE | ||
| 520 | |a Sodium boro[3H]hydride reduction of tyrosine decarboxylase from Streptococcus faecalis followed by complete hydrolysis of the enzyme produces epsilon-[3H]pyridoxyllysine. Degradation of this material to [4'-3H]pyridoxamine and stereochemical analysis with apoaspartate aminotransferase shows that the re side at C-4' of the cofactor is exposed to solvent at pH 5.5 and 7.0. After binding of L-tyrosine at pH 5.5 or tyramine at pH 7.0 to the holoenzyme, sodium boro[3H]hydride reduction proceeds from the si face at C-4' of the substrate . cofactor complex. This indicates one of two conformational changes occurs upon binding of substrate; either rotation about the C-4 to C-4' bond in the cofactor or rotation about the axis through the C-5 and C-5' bond | ||
| 650 | 4 | |a Journal Article | |
| 650 | 7 | |a Borohydrides |2 NLM | |
| 650 | 7 | |a Pyridoxal |2 NLM | |
| 650 | 7 | |a 3THM379K8A |2 NLM | |
| 650 | 7 | |a Tyrosine Decarboxylase |2 NLM | |
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| 700 | 1 | |a Sellers, H W |e verfasserin |4 aut | |
| 773 | 0 | 8 | |i Enthalten in |t The Journal of biological chemistry |d 1945 |g 254(1979), 12 vom: 25. Juni, Seite 5053-7 |w (DE-627)NLM000004995 |x 1083-351X |7 nnns |
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