Role of a highly conserved proline-126 in ThDP binding of Mycobacterium tuberculosis acetohydroxyacid synthase
• Possible role of a highly conserved P126 of AHAS was evaluated by mutagenesis. • The mutated proteins, P126V, P126T, P126A, and P126E,exhibits lower activities. • P126 is located in the ThDP binding pocket of M. tuberculosis AHAS homology model. • Modeling and kinetics results suggest significant...
Ausführliche Beschreibung
Gespeichert in:
| Autor*in: |
Baig, Irshad Ahmed [verfasserIn] |
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E-Artikel |
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Englisch |
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2013 |
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7 |
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Enthalten in: Robust variable selection and estimation via adaptive elastic net S-estimators for linear regression - Kepplinger, David ELSEVIER, 2023, biotechnology research and reviews, Amsterdam [u.a.] |
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| Übergeordnetes Werk: |
volume:53 ; year:2013 ; number:4 ; day:10 ; month:09 ; pages:243-249 ; extent:7 |
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10.1016/j.enzmictec.2013.05.006 |
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| 520 | |a • Possible role of a highly conserved P126 of AHAS was evaluated by mutagenesis. • The mutated proteins, P126V, P126T, P126A, and P126E,exhibits lower activities. • P126 is located in the ThDP binding pocket of M. tuberculosis AHAS homology model. • Modeling and kinetics results suggest significant role for P126 in ThDP binding. | ||
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role of a highly conserved proline-126 in thdp binding of mycobacterium tuberculosis acetohydroxyacid synthase |
| title_auth |
Role of a highly conserved proline-126 in ThDP binding of Mycobacterium tuberculosis acetohydroxyacid synthase |
| abstract |
• Possible role of a highly conserved P126 of AHAS was evaluated by mutagenesis. • The mutated proteins, P126V, P126T, P126A, and P126E,exhibits lower activities. • P126 is located in the ThDP binding pocket of M. tuberculosis AHAS homology model. • Modeling and kinetics results suggest significant role for P126 in ThDP binding. |
| abstractGer |
• Possible role of a highly conserved P126 of AHAS was evaluated by mutagenesis. • The mutated proteins, P126V, P126T, P126A, and P126E,exhibits lower activities. • P126 is located in the ThDP binding pocket of M. tuberculosis AHAS homology model. • Modeling and kinetics results suggest significant role for P126 in ThDP binding. |
| abstract_unstemmed |
• Possible role of a highly conserved P126 of AHAS was evaluated by mutagenesis. • The mutated proteins, P126V, P126T, P126A, and P126E,exhibits lower activities. • P126 is located in the ThDP binding pocket of M. tuberculosis AHAS homology model. • Modeling and kinetics results suggest significant role for P126 in ThDP binding. |
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4 |
| title_short |
Role of a highly conserved proline-126 in ThDP binding of Mycobacterium tuberculosis acetohydroxyacid synthase |
| url |
https://doi.org/10.1016/j.enzmictec.2013.05.006 |
| remote_bool |
true |
| author2 |
Gedi, Vinayakumar Lee, Sang-Choon Koh, Seong-Ho Yoon, Moon-Young |
| author2Str |
Gedi, Vinayakumar Lee, Sang-Choon Koh, Seong-Ho Yoon, Moon-Young |
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| doi_str |
10.1016/j.enzmictec.2013.05.006 |
| up_date |
2024-07-06T20:52:02.432Z |
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