Phenylalanine/tyrosine ammonia-lyase: Difference between revisions

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Phenylalanine/tyrosine ammonia-lyase
Phenylalanine/tyrosine ammonia-lyase
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EC no.	4.3.1.25
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BRENDA	BRENDA entry
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Revision as of 21:52, 28 August 2016

Phenylalanine/tyrosine ammonia-lyase (EC 4.3.1.25, PTAL, bifunctional PAL) is an enzyme with systematic name L-phenylalanine(or L-tyrosine):trans-cinnamate(or trans-p-hydroxycinnamate) ammonia-lyase.^[1]^[2]^[3]^[4]^[5] This enzyme catalyses the following chemical reaction

(1) L-phenylalanine

\rightleftharpoons

trans-cinnamate + NH₃

(2) L-tyrosine

\rightleftharpoons

trans-p-hydroxycinnamate + NH₃

This enzyme is a member of the aromatic amino acid lyase family.

References

^ Rösler, J.; Krekel, F.; Amrhein, N.; Schmid, J. (1997). "Maize phenylalanine ammonia-lyase has tyrosine ammonia-lyase activity". Plant Physiol. 113: 175–179. doi:10.1104/pp.113.1.175. PMID 9008393.
^ Watts, K.T.; Mijts, B.N.; Lee, P.C.; Manning, A.J.; Schmidt-Dannert, C. (2006). "Discovery of a substrate selectivity switch in tyrosine ammonia-lyase, a member of the aromatic amino acid lyase family". Chem. Biol. 13: 1317–1326. doi:10.1016/j.chembiol.2006.10.008. PMID 17185227.
^ Louie, G.V.; Bowman, M.E.; Moffitt, M.C.; Baiga, T.J.; Moore, B.S.; Noel, J.P. (2006). "Structural determinants and modulation of substrate specificity in phenylalanine-tyrosine ammonia-lyases". Chem. Biol. 13: 1327–1338. doi:10.1016/j.chembiol.2006.11.011. PMID 17185228.
^ Schwede, T.F.; Rétey, J.; Schulz, G.E. (1999). "Crystal structure of histidine ammonia-lyase revealing a novel polypeptide modification as the catalytic electrophile". Biochemistry. 38: 5355–5361. doi:10.1021/bi982929q. PMID 10220322.
^ Barros, J.; Serrani-Yarce, J.C.; Chen, F.; Baxter, D.; Venables, B.J.; Dixon, R.A. (2016). "Role of bifunctional ammonia-lyase in grass cell wall biosynthesis". Nat. Plants 2: 16050. doi:10.1038/nplants.2016.50

External links

Phenylalanine/tyrosine+ammonia-lyase at the U.S. National Library of Medicine Medical Subject Headings (MeSH)

[1] Rösler, J.; Krekel, F.; Amrhein, N.; Schmid, J. (1997). "Maize phenylalanine ammonia-lyase has tyrosine ammonia-lyase activity". Plant Physiol. 113: 175–179. doi:10.1104/pp.113.1.175. PMID 9008393.

[2] Watts, K.T.; Mijts, B.N.; Lee, P.C.; Manning, A.J.; Schmidt-Dannert, C. (2006). "Discovery of a substrate selectivity switch in tyrosine ammonia-lyase, a member of the aromatic amino acid lyase family". Chem. Biol. 13: 1317–1326. doi:10.1016/j.chembiol.2006.10.008. PMID 17185227.

[3] Louie, G.V.; Bowman, M.E.; Moffitt, M.C.; Baiga, T.J.; Moore, B.S.; Noel, J.P. (2006). "Structural determinants and modulation of substrate specificity in phenylalanine-tyrosine ammonia-lyases". Chem. Biol. 13: 1327–1338. doi:10.1016/j.chembiol.2006.11.011. PMID 17185228.

[4] Schwede, T.F.; Rétey, J.; Schulz, G.E. (1999). "Crystal structure of histidine ammonia-lyase revealing a novel polypeptide modification as the catalytic electrophile". Biochemistry. 38: 5355–5361. doi:10.1021/bi982929q. PMID 10220322.

[5] Barros, J.; Serrani-Yarce, J.C.; Chen, F.; Baxter, D.; Venables, B.J.; Dixon, R.A. (2016). "Role of bifunctional ammonia-lyase in grass cell wall biosynthesis". Nat. Plants 2: 16050. doi:10.1038/nplants.2016.50

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-'''Phenylalanine/tyrosine ammonia-lyase''' ({{EC number|4.3.1.25}}, ''PTAL'', ''bifunctional PAL'') is an [[enzyme]] with [[List of enzymes|systematic name]] ''L-phenylalanine(or L-tyrosine):trans-cinnamate(or trans-p-hydroxycinnamate) ammonia-lyase''.<ref>{{cite journal | title = Maize phenylalanine ammonia-lyase has tyrosine ammonia-lyase activity |author1 = Rösler, J. |author2 =Krekel, F. |author3 =Amrhein, N. |author4 =Schmid, J. |journal = Plant Physiol. |date = 1997 |volume = 113 |pages = 175–179 |pmid = 9008393 |doi=10.1104/pp.113.1.175}}</ref><ref>{{cite journal | title = Discovery of a substrate selectivity switch in tyrosine ammonia-lyase, a member of the aromatic amino acid lyase family |author1 = Watts, K.T. |author2 =Mijts, B.N. |author3 =Lee, P.C. |author4 =Manning, A.J. |author5 =Schmidt-Dannert, C. |journal = Chem. Biol. |date = 2006 |volume = 13 |pages = 1317–1326 |pmid = 17185227 |doi=10.1016/j.chembiol.2006.10.008}}</ref><ref>{{cite journal | title = Structural determinants and modulation of substrate specificity in phenylalanine-tyrosine ammonia-lyases |author1 = Louie, G.V. |author2 =Bowman, M.E. |author3 =Moffitt, M.C. |author4 =Baiga, T.J. |author5 =Moore, B.S. |author6 =Noel, J.P. | journal = Chem. Biol. |date = 2006 |volume = 13 |pages = 1327–1338 |pmid = 17185228 |doi=10.1016/j.chembiol.2006.11.011}}</ref><ref>{{cite journal | title = Crystal structure of histidine ammonia-lyase revealing a novel polypeptide modification as the catalytic electrophile |author1 = Schwede, T.F. |author2 =Rétey, J. |author3 =Schulz, G.E. |journal = Biochemistry |date = 1999 |volume = 38 |pages = 5355–5361 |pmid = 10220322 |doi=10.1021/bi982929q}}</ref> This enzyme [[catalysis|catalyses]] the following [[chemical reaction]]
+'''Phenylalanine/tyrosine ammonia-lyase''' ({{EC number|4.3.1.25}}, ''PTAL'', ''bifunctional PAL'') is an [[enzyme]] with [[List of enzymes|systematic name]] ''L-phenylalanine(or L-tyrosine):trans-cinnamate(or trans-p-hydroxycinnamate) ammonia-lyase''.<ref>{{cite journal | title = Maize phenylalanine ammonia-lyase has tyrosine ammonia-lyase activity |author1 = Rösler, J. |author2 =Krekel, F. |author3 =Amrhein, N. |author4 =Schmid, J. |journal = Plant Physiol. |date = 1997 |volume = 113 |pages = 175–179 |pmid = 9008393 |doi=10.1104/pp.113.1.175}}</ref><ref>{{cite journal | title = Discovery of a substrate selectivity switch in tyrosine ammonia-lyase, a member of the aromatic amino acid lyase family |author1 = Watts, K.T. |author2 =Mijts, B.N. |author3 =Lee, P.C. |author4 =Manning, A.J. |author5 =Schmidt-Dannert, C. |journal = Chem. Biol. |date = 2006 |volume = 13 |pages = 1317–1326 |pmid = 17185227 |doi=10.1016/j.chembiol.2006.10.008}}</ref><ref>{{cite journal | title = Structural determinants and modulation of substrate specificity in phenylalanine-tyrosine ammonia-lyases |author1 = Louie, G.V. |author2 =Bowman, M.E. |author3 =Moffitt, M.C. |author4 =Baiga, T.J. |author5 =Moore, B.S. |author6 =Noel, J.P. | journal = Chem. Biol. |date = 2006 |volume = 13 |pages = 1327–1338 |pmid = 17185228 |doi=10.1016/j.chembiol.2006.11.011}}</ref><ref>{{cite journal | title = Crystal structure of histidine ammonia-lyase revealing a novel polypeptide modification as the catalytic electrophile |author1 = Schwede, T.F. |author2 =Rétey, J. |author3 =Schulz, G.E. |journal = Biochemistry |date = 1999 |volume = 38 |pages = 5355–5361 |pmid = 10220322 |doi=10.1021/bi982929q}}</ref><ref>Barros, J.; Serrani-Yarce, J.C.; Chen, F.; Baxter, D.; Venables, B.J.; Dixon, R.A. (2016). "Role of bifunctional ammonia-lyase in grass cell wall biosynthesis". ''Nat. Plants'' '''2''': 16050. <abbr>doi</abbr>:10.1038/nplants.2016.50 </ref> This enzyme [[catalysis|catalyses]] the following [[chemical reaction]]
 : (1) L-[[phenylalanine]] <math>\rightleftharpoons</math> [[trans-cinnamate]] + NH<sub>3</sub>

v t e Carbon–nitrogen lyases (EC 4.3)
4.3.1: ammonia-lyases	Histidine ammonia-lyase Formiminotransferase cyclodeaminase Serine dehydratase Phenylalanine ammonia-lyase
4.3.2: amidine-lyases	Argininosuccinate lyase Adenylosuccinate lyase

v t e Enzymes
Activity	Active site Binding site Catalytic triad Oxyanion hole Enzyme promiscuity Diffusion-limited enzyme Cofactor Enzyme catalysis
Regulation	Allosteric regulation Cooperativity Enzyme inhibitor Enzyme activator
Classification	EC number Enzyme superfamily Enzyme family List of enzymes
Kinetics	Enzyme kinetics Eadie–Hofstee diagram Hanes–Woolf plot Lineweaver–Burk plot Michaelis–Menten kinetics
Types	EC1 Oxidoreductases (list) EC2 Transferases (list) EC3 Hydrolases (list) EC4 Lyases (list) EC5 Isomerases (list) EC6 Ligases (list) EC7 Translocases (list)