Insights into the substrate selectivity of
The Bambusa oldhamii phenylalanine ammonia-lyase (PAL) proteins, BoPAL1 and BoPAL2, exhibited different substrate specificities toward phenylalanine (Phe) and tyrosine (Tyr). Mutational analysis was conducted to study their substrate selectivity. All expressed wild-type and mutant BoPAL proteins man...
Ausführliche Beschreibung
Gespeichert in:
| Autor*in: |
Hsieh, Chun-Yen [verfasserIn] Huang, Yi-Hao [verfasserIn] Lin, Zhih-Yu [verfasserIn] Hsieh, Lu-Sheng [verfasserIn] |
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| Format: |
E-Artikel |
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| Sprache: |
Englisch |
| Erschienen: |
2020 |
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| Schlagwörter: |
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| Übergeordnetes Werk: |
Enthalten in: Phytochemistry letters - Amsterdam [u.a.] : Elsevier, 2008, 38, Seite 140-143 |
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| Übergeordnetes Werk: |
volume:38 ; pages:140-143 |
| DOI / URN: |
10.1016/j.phytol.2020.06.002 |
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| Katalog-ID: |
ELV004407415 |
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| 245 | 1 | 0 | |a Insights into the substrate selectivity of |
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| 520 | |a The Bambusa oldhamii phenylalanine ammonia-lyase (PAL) proteins, BoPAL1 and BoPAL2, exhibited different substrate specificities toward phenylalanine (Phe) and tyrosine (Tyr). Mutational analysis was conducted to study their substrate selectivity. All expressed wild-type and mutant BoPAL proteins manifested PAL activity; however, K m and k cat values were varied. BoPAL1 F133H and BoPAL2 F134H showed decreased k cat/K m values toward phenylalanine and significantly increased tyrosine ammonia-lyase (TAL) activities. BoPAL1 V197I and BoPAL2 I198 V showed opposite results regarding TAL activity, indicating that the Val or Ile residue prior to the active site, Ala-Ser-Gly, is essential for modulating Phe/Tyr substrate selectivity. | ||
| 650 | 4 | |a Phenylalanine ammonia-lyase | |
| 650 | 4 | |a phenylalanine/tyrosine ammonia-lyase | |
| 650 | 4 | |a Site-directed mutagenesis | |
| 650 | 4 | |a Substrate selectivity | |
| 650 | 4 | |a Tyrosine ammonia-lyase | |
| 700 | 1 | |a Huang, Yi-Hao |e verfasserin |4 aut | |
| 700 | 1 | |a Lin, Zhih-Yu |e verfasserin |4 aut | |
| 700 | 1 | |a Hsieh, Lu-Sheng |e verfasserin |4 aut | |
| 773 | 0 | 8 | |i Enthalten in |t Phytochemistry letters |d Amsterdam [u.a.] : Elsevier, 2008 |g 38, Seite 140-143 |h Online-Ressource |w (DE-627)566010879 |w (DE-600)2425258-X |w (DE-576)294350659 |x 1874-3900 |7 nnns |
| 773 | 1 | 8 | |g volume:38 |g pages:140-143 |
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| 912 | |a SYSFLAG_U | ||
| 912 | |a GBV_ELV | ||
| 912 | |a FID-BIODIV | ||
| 912 | |a SSG-OLC-PHA | ||
| 912 | |a GBV_ILN_20 | ||
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| 912 | |a GBV_ILN_31 | ||
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| 912 | |a GBV_ILN_40 | ||
| 912 | |a GBV_ILN_60 | ||
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| 912 | |a GBV_ILN_63 | ||
| 912 | |a GBV_ILN_65 | ||
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| 912 | |a GBV_ILN_74 | ||
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| 912 | |a GBV_ILN_100 | ||
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| 912 | |a GBV_ILN_105 | ||
| 912 | |a GBV_ILN_110 | ||
| 912 | |a GBV_ILN_150 | ||
| 912 | |a GBV_ILN_151 | ||
| 912 | |a GBV_ILN_224 | ||
| 912 | |a GBV_ILN_370 | ||
| 912 | |a GBV_ILN_602 | ||
| 912 | |a GBV_ILN_702 | ||
| 912 | |a GBV_ILN_2003 | ||
| 912 | |a GBV_ILN_2004 | ||
| 912 | |a GBV_ILN_2005 | ||
| 912 | |a GBV_ILN_2006 | ||
| 912 | |a GBV_ILN_2008 | ||
| 912 | |a GBV_ILN_2011 | ||
| 912 | |a GBV_ILN_2014 | ||
| 912 | |a GBV_ILN_2015 | ||
| 912 | |a GBV_ILN_2020 | ||
| 912 | |a GBV_ILN_2021 | ||
| 912 | |a GBV_ILN_2025 | ||
| 912 | |a GBV_ILN_2027 | ||
| 912 | |a GBV_ILN_2034 | ||
| 912 | |a GBV_ILN_2038 | ||
| 912 | |a GBV_ILN_2044 | ||
| 912 | |a GBV_ILN_2048 | ||
| 912 | |a GBV_ILN_2049 | ||
| 912 | |a GBV_ILN_2050 | ||
| 912 | |a GBV_ILN_2056 | ||
| 912 | |a GBV_ILN_2059 | ||
| 912 | |a GBV_ILN_2061 | ||
| 912 | |a GBV_ILN_2064 | ||
| 912 | |a GBV_ILN_2065 | ||
| 912 | |a GBV_ILN_2068 | ||
| 912 | |a GBV_ILN_2088 | ||
| 912 | |a GBV_ILN_2111 | ||
| 912 | |a GBV_ILN_2112 | ||
| 912 | |a GBV_ILN_2113 | ||
| 912 | |a GBV_ILN_2118 | ||
| 912 | |a GBV_ILN_2122 | ||
| 912 | |a GBV_ILN_2129 | ||
| 912 | |a GBV_ILN_2143 | ||
| 912 | |a GBV_ILN_2147 | ||
| 912 | |a GBV_ILN_2148 | ||
| 912 | |a GBV_ILN_2152 | ||
| 912 | |a GBV_ILN_2153 | ||
| 912 | |a GBV_ILN_2190 | ||
| 912 | |a GBV_ILN_2470 | ||
| 912 | |a GBV_ILN_2507 | ||
| 912 | |a GBV_ILN_2522 | ||
| 912 | |a GBV_ILN_4035 | ||
| 912 | |a GBV_ILN_4037 | ||
| 912 | |a GBV_ILN_4046 | ||
| 912 | |a GBV_ILN_4112 | ||
| 912 | |a GBV_ILN_4125 | ||
| 912 | |a GBV_ILN_4126 | ||
| 912 | |a GBV_ILN_4242 | ||
| 912 | |a GBV_ILN_4251 | ||
| 912 | |a GBV_ILN_4305 | ||
| 912 | |a GBV_ILN_4313 | ||
| 912 | |a GBV_ILN_4322 | ||
| 912 | |a GBV_ILN_4323 | ||
| 912 | |a GBV_ILN_4324 | ||
| 912 | |a GBV_ILN_4325 | ||
| 912 | |a GBV_ILN_4326 | ||
| 912 | |a GBV_ILN_4333 | ||
| 912 | |a GBV_ILN_4334 | ||
| 912 | |a GBV_ILN_4335 | ||
| 912 | |a GBV_ILN_4338 | ||
| 912 | |a GBV_ILN_4393 | ||
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2020 |
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2020 |
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10.1016/j.phytol.2020.06.002 doi (DE-627)ELV004407415 (ELSEVIER)S1874-3900(20)30165-8 DE-627 ger DE-627 rda eng 580 540 DE-600 BIODIV DE-30 fid Hsieh, Chun-Yen verfasserin aut Insights into the substrate selectivity of 2020 nicht spezifiziert zzz rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier The Bambusa oldhamii phenylalanine ammonia-lyase (PAL) proteins, BoPAL1 and BoPAL2, exhibited different substrate specificities toward phenylalanine (Phe) and tyrosine (Tyr). Mutational analysis was conducted to study their substrate selectivity. All expressed wild-type and mutant BoPAL proteins manifested PAL activity; however, K m and k cat values were varied. BoPAL1 F133H and BoPAL2 F134H showed decreased k cat/K m values toward phenylalanine and significantly increased tyrosine ammonia-lyase (TAL) activities. BoPAL1 V197I and BoPAL2 I198 V showed opposite results regarding TAL activity, indicating that the Val or Ile residue prior to the active site, Ala-Ser-Gly, is essential for modulating Phe/Tyr substrate selectivity. Phenylalanine ammonia-lyase phenylalanine/tyrosine ammonia-lyase Site-directed mutagenesis Substrate selectivity Tyrosine ammonia-lyase Huang, Yi-Hao verfasserin aut Lin, Zhih-Yu verfasserin aut Hsieh, Lu-Sheng verfasserin aut Enthalten in Phytochemistry letters Amsterdam [u.a.] : Elsevier, 2008 38, Seite 140-143 Online-Ressource (DE-627)566010879 (DE-600)2425258-X (DE-576)294350659 1874-3900 nnns volume:38 pages:140-143 GBV_USEFLAG_U SYSFLAG_U GBV_ELV FID-BIODIV SSG-OLC-PHA GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_32 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_74 GBV_ILN_90 GBV_ILN_95 GBV_ILN_100 GBV_ILN_101 GBV_ILN_105 GBV_ILN_110 GBV_ILN_150 GBV_ILN_151 GBV_ILN_224 GBV_ILN_370 GBV_ILN_602 GBV_ILN_702 GBV_ILN_2003 GBV_ILN_2004 GBV_ILN_2005 GBV_ILN_2006 GBV_ILN_2008 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2015 GBV_ILN_2020 GBV_ILN_2021 GBV_ILN_2025 GBV_ILN_2027 GBV_ILN_2034 GBV_ILN_2038 GBV_ILN_2044 GBV_ILN_2048 GBV_ILN_2049 GBV_ILN_2050 GBV_ILN_2056 GBV_ILN_2059 GBV_ILN_2061 GBV_ILN_2064 GBV_ILN_2065 GBV_ILN_2068 GBV_ILN_2088 GBV_ILN_2111 GBV_ILN_2112 GBV_ILN_2113 GBV_ILN_2118 GBV_ILN_2122 GBV_ILN_2129 GBV_ILN_2143 GBV_ILN_2147 GBV_ILN_2148 GBV_ILN_2152 GBV_ILN_2153 GBV_ILN_2190 GBV_ILN_2470 GBV_ILN_2507 GBV_ILN_2522 GBV_ILN_4035 GBV_ILN_4037 GBV_ILN_4046 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4242 GBV_ILN_4251 GBV_ILN_4305 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4326 GBV_ILN_4333 GBV_ILN_4334 GBV_ILN_4335 GBV_ILN_4338 GBV_ILN_4393 AR 38 140-143 |
| spelling |
10.1016/j.phytol.2020.06.002 doi (DE-627)ELV004407415 (ELSEVIER)S1874-3900(20)30165-8 DE-627 ger DE-627 rda eng 580 540 DE-600 BIODIV DE-30 fid Hsieh, Chun-Yen verfasserin aut Insights into the substrate selectivity of 2020 nicht spezifiziert zzz rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier The Bambusa oldhamii phenylalanine ammonia-lyase (PAL) proteins, BoPAL1 and BoPAL2, exhibited different substrate specificities toward phenylalanine (Phe) and tyrosine (Tyr). Mutational analysis was conducted to study their substrate selectivity. All expressed wild-type and mutant BoPAL proteins manifested PAL activity; however, K m and k cat values were varied. BoPAL1 F133H and BoPAL2 F134H showed decreased k cat/K m values toward phenylalanine and significantly increased tyrosine ammonia-lyase (TAL) activities. BoPAL1 V197I and BoPAL2 I198 V showed opposite results regarding TAL activity, indicating that the Val or Ile residue prior to the active site, Ala-Ser-Gly, is essential for modulating Phe/Tyr substrate selectivity. Phenylalanine ammonia-lyase phenylalanine/tyrosine ammonia-lyase Site-directed mutagenesis Substrate selectivity Tyrosine ammonia-lyase Huang, Yi-Hao verfasserin aut Lin, Zhih-Yu verfasserin aut Hsieh, Lu-Sheng verfasserin aut Enthalten in Phytochemistry letters Amsterdam [u.a.] : Elsevier, 2008 38, Seite 140-143 Online-Ressource (DE-627)566010879 (DE-600)2425258-X (DE-576)294350659 1874-3900 nnns volume:38 pages:140-143 GBV_USEFLAG_U SYSFLAG_U GBV_ELV FID-BIODIV SSG-OLC-PHA GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_32 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_74 GBV_ILN_90 GBV_ILN_95 GBV_ILN_100 GBV_ILN_101 GBV_ILN_105 GBV_ILN_110 GBV_ILN_150 GBV_ILN_151 GBV_ILN_224 GBV_ILN_370 GBV_ILN_602 GBV_ILN_702 GBV_ILN_2003 GBV_ILN_2004 GBV_ILN_2005 GBV_ILN_2006 GBV_ILN_2008 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2015 GBV_ILN_2020 GBV_ILN_2021 GBV_ILN_2025 GBV_ILN_2027 GBV_ILN_2034 GBV_ILN_2038 GBV_ILN_2044 GBV_ILN_2048 GBV_ILN_2049 GBV_ILN_2050 GBV_ILN_2056 GBV_ILN_2059 GBV_ILN_2061 GBV_ILN_2064 GBV_ILN_2065 GBV_ILN_2068 GBV_ILN_2088 GBV_ILN_2111 GBV_ILN_2112 GBV_ILN_2113 GBV_ILN_2118 GBV_ILN_2122 GBV_ILN_2129 GBV_ILN_2143 GBV_ILN_2147 GBV_ILN_2148 GBV_ILN_2152 GBV_ILN_2153 GBV_ILN_2190 GBV_ILN_2470 GBV_ILN_2507 GBV_ILN_2522 GBV_ILN_4035 GBV_ILN_4037 GBV_ILN_4046 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4242 GBV_ILN_4251 GBV_ILN_4305 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4326 GBV_ILN_4333 GBV_ILN_4334 GBV_ILN_4335 GBV_ILN_4338 GBV_ILN_4393 AR 38 140-143 |
| allfields_unstemmed |
10.1016/j.phytol.2020.06.002 doi (DE-627)ELV004407415 (ELSEVIER)S1874-3900(20)30165-8 DE-627 ger DE-627 rda eng 580 540 DE-600 BIODIV DE-30 fid Hsieh, Chun-Yen verfasserin aut Insights into the substrate selectivity of 2020 nicht spezifiziert zzz rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier The Bambusa oldhamii phenylalanine ammonia-lyase (PAL) proteins, BoPAL1 and BoPAL2, exhibited different substrate specificities toward phenylalanine (Phe) and tyrosine (Tyr). Mutational analysis was conducted to study their substrate selectivity. All expressed wild-type and mutant BoPAL proteins manifested PAL activity; however, K m and k cat values were varied. BoPAL1 F133H and BoPAL2 F134H showed decreased k cat/K m values toward phenylalanine and significantly increased tyrosine ammonia-lyase (TAL) activities. BoPAL1 V197I and BoPAL2 I198 V showed opposite results regarding TAL activity, indicating that the Val or Ile residue prior to the active site, Ala-Ser-Gly, is essential for modulating Phe/Tyr substrate selectivity. Phenylalanine ammonia-lyase phenylalanine/tyrosine ammonia-lyase Site-directed mutagenesis Substrate selectivity Tyrosine ammonia-lyase Huang, Yi-Hao verfasserin aut Lin, Zhih-Yu verfasserin aut Hsieh, Lu-Sheng verfasserin aut Enthalten in Phytochemistry letters Amsterdam [u.a.] : Elsevier, 2008 38, Seite 140-143 Online-Ressource (DE-627)566010879 (DE-600)2425258-X (DE-576)294350659 1874-3900 nnns volume:38 pages:140-143 GBV_USEFLAG_U SYSFLAG_U GBV_ELV FID-BIODIV SSG-OLC-PHA GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_32 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_74 GBV_ILN_90 GBV_ILN_95 GBV_ILN_100 GBV_ILN_101 GBV_ILN_105 GBV_ILN_110 GBV_ILN_150 GBV_ILN_151 GBV_ILN_224 GBV_ILN_370 GBV_ILN_602 GBV_ILN_702 GBV_ILN_2003 GBV_ILN_2004 GBV_ILN_2005 GBV_ILN_2006 GBV_ILN_2008 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2015 GBV_ILN_2020 GBV_ILN_2021 GBV_ILN_2025 GBV_ILN_2027 GBV_ILN_2034 GBV_ILN_2038 GBV_ILN_2044 GBV_ILN_2048 GBV_ILN_2049 GBV_ILN_2050 GBV_ILN_2056 GBV_ILN_2059 GBV_ILN_2061 GBV_ILN_2064 GBV_ILN_2065 GBV_ILN_2068 GBV_ILN_2088 GBV_ILN_2111 GBV_ILN_2112 GBV_ILN_2113 GBV_ILN_2118 GBV_ILN_2122 GBV_ILN_2129 GBV_ILN_2143 GBV_ILN_2147 GBV_ILN_2148 GBV_ILN_2152 GBV_ILN_2153 GBV_ILN_2190 GBV_ILN_2470 GBV_ILN_2507 GBV_ILN_2522 GBV_ILN_4035 GBV_ILN_4037 GBV_ILN_4046 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4242 GBV_ILN_4251 GBV_ILN_4305 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4326 GBV_ILN_4333 GBV_ILN_4334 GBV_ILN_4335 GBV_ILN_4338 GBV_ILN_4393 AR 38 140-143 |
| allfieldsGer |
10.1016/j.phytol.2020.06.002 doi (DE-627)ELV004407415 (ELSEVIER)S1874-3900(20)30165-8 DE-627 ger DE-627 rda eng 580 540 DE-600 BIODIV DE-30 fid Hsieh, Chun-Yen verfasserin aut Insights into the substrate selectivity of 2020 nicht spezifiziert zzz rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier The Bambusa oldhamii phenylalanine ammonia-lyase (PAL) proteins, BoPAL1 and BoPAL2, exhibited different substrate specificities toward phenylalanine (Phe) and tyrosine (Tyr). Mutational analysis was conducted to study their substrate selectivity. All expressed wild-type and mutant BoPAL proteins manifested PAL activity; however, K m and k cat values were varied. BoPAL1 F133H and BoPAL2 F134H showed decreased k cat/K m values toward phenylalanine and significantly increased tyrosine ammonia-lyase (TAL) activities. BoPAL1 V197I and BoPAL2 I198 V showed opposite results regarding TAL activity, indicating that the Val or Ile residue prior to the active site, Ala-Ser-Gly, is essential for modulating Phe/Tyr substrate selectivity. Phenylalanine ammonia-lyase phenylalanine/tyrosine ammonia-lyase Site-directed mutagenesis Substrate selectivity Tyrosine ammonia-lyase Huang, Yi-Hao verfasserin aut Lin, Zhih-Yu verfasserin aut Hsieh, Lu-Sheng verfasserin aut Enthalten in Phytochemistry letters Amsterdam [u.a.] : Elsevier, 2008 38, Seite 140-143 Online-Ressource (DE-627)566010879 (DE-600)2425258-X (DE-576)294350659 1874-3900 nnns volume:38 pages:140-143 GBV_USEFLAG_U SYSFLAG_U GBV_ELV FID-BIODIV SSG-OLC-PHA GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_32 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_74 GBV_ILN_90 GBV_ILN_95 GBV_ILN_100 GBV_ILN_101 GBV_ILN_105 GBV_ILN_110 GBV_ILN_150 GBV_ILN_151 GBV_ILN_224 GBV_ILN_370 GBV_ILN_602 GBV_ILN_702 GBV_ILN_2003 GBV_ILN_2004 GBV_ILN_2005 GBV_ILN_2006 GBV_ILN_2008 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2015 GBV_ILN_2020 GBV_ILN_2021 GBV_ILN_2025 GBV_ILN_2027 GBV_ILN_2034 GBV_ILN_2038 GBV_ILN_2044 GBV_ILN_2048 GBV_ILN_2049 GBV_ILN_2050 GBV_ILN_2056 GBV_ILN_2059 GBV_ILN_2061 GBV_ILN_2064 GBV_ILN_2065 GBV_ILN_2068 GBV_ILN_2088 GBV_ILN_2111 GBV_ILN_2112 GBV_ILN_2113 GBV_ILN_2118 GBV_ILN_2122 GBV_ILN_2129 GBV_ILN_2143 GBV_ILN_2147 GBV_ILN_2148 GBV_ILN_2152 GBV_ILN_2153 GBV_ILN_2190 GBV_ILN_2470 GBV_ILN_2507 GBV_ILN_2522 GBV_ILN_4035 GBV_ILN_4037 GBV_ILN_4046 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4242 GBV_ILN_4251 GBV_ILN_4305 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4326 GBV_ILN_4333 GBV_ILN_4334 GBV_ILN_4335 GBV_ILN_4338 GBV_ILN_4393 AR 38 140-143 |
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insights into the substrate selectivity of |
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| abstract |
The Bambusa oldhamii phenylalanine ammonia-lyase (PAL) proteins, BoPAL1 and BoPAL2, exhibited different substrate specificities toward phenylalanine (Phe) and tyrosine (Tyr). Mutational analysis was conducted to study their substrate selectivity. All expressed wild-type and mutant BoPAL proteins manifested PAL activity; however, K m and k cat values were varied. BoPAL1 F133H and BoPAL2 F134H showed decreased k cat/K m values toward phenylalanine and significantly increased tyrosine ammonia-lyase (TAL) activities. BoPAL1 V197I and BoPAL2 I198 V showed opposite results regarding TAL activity, indicating that the Val or Ile residue prior to the active site, Ala-Ser-Gly, is essential for modulating Phe/Tyr substrate selectivity. |
| abstractGer |
The Bambusa oldhamii phenylalanine ammonia-lyase (PAL) proteins, BoPAL1 and BoPAL2, exhibited different substrate specificities toward phenylalanine (Phe) and tyrosine (Tyr). Mutational analysis was conducted to study their substrate selectivity. All expressed wild-type and mutant BoPAL proteins manifested PAL activity; however, K m and k cat values were varied. BoPAL1 F133H and BoPAL2 F134H showed decreased k cat/K m values toward phenylalanine and significantly increased tyrosine ammonia-lyase (TAL) activities. BoPAL1 V197I and BoPAL2 I198 V showed opposite results regarding TAL activity, indicating that the Val or Ile residue prior to the active site, Ala-Ser-Gly, is essential for modulating Phe/Tyr substrate selectivity. |
| abstract_unstemmed |
The Bambusa oldhamii phenylalanine ammonia-lyase (PAL) proteins, BoPAL1 and BoPAL2, exhibited different substrate specificities toward phenylalanine (Phe) and tyrosine (Tyr). Mutational analysis was conducted to study their substrate selectivity. All expressed wild-type and mutant BoPAL proteins manifested PAL activity; however, K m and k cat values were varied. BoPAL1 F133H and BoPAL2 F134H showed decreased k cat/K m values toward phenylalanine and significantly increased tyrosine ammonia-lyase (TAL) activities. BoPAL1 V197I and BoPAL2 I198 V showed opposite results regarding TAL activity, indicating that the Val or Ile residue prior to the active site, Ala-Ser-Gly, is essential for modulating Phe/Tyr substrate selectivity. |
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