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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PDB structures	RCSB PDB PDBe PDBsum
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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 (January 1997). "Maize phenylalanine ammonia-lyase has tyrosine ammonia-lyase activity". Plant Physiology. 113 (1): 175–9. doi:10.1104/pp.113.1.175. PMC 158128. PMID 9008393.
^ Watts KT, Mijts BN, Lee PC, Manning AJ, Schmidt-Dannert C (December 2006). "Discovery of a substrate selectivity switch in tyrosine ammonia-lyase, a member of the aromatic amino acid lyase family". Chemistry & Biology. 13 (12): 1317–26. doi:10.1016/j.chembiol.2006.10.008. PMID 17185227.
^ Louie GV, Bowman ME, Moffitt MC, Baiga TJ, Moore BS, Noel JP (December 2006). "Structural determinants and modulation of substrate specificity in phenylalanine-tyrosine ammonia-lyases". Chemistry & Biology. 13 (12): 1327–38. doi:10.1016/j.chembiol.2006.11.011. PMC 2859959. PMID 17185228.
^ Schwede TF, Rétey J, Schulz GE (April 1999). "Crystal structure of histidine ammonia-lyase revealing a novel polypeptide modification as the catalytic electrophile". Biochemistry. 38 (17): 5355–61. doi:10.1021/bi982929q. PMID 10220322.
^ Barros J, Serrani-Yarce JC, Chen F, Baxter D, Venables BJ, Dixon RA (May 2016). "Role of bifunctional ammonia-lyase in grass cell wall biosynthesis". Nature Plants. 2 (6): 16050. doi:10.1038/nplants.2016.50. PMID 27255834.

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 (January 1997). "Maize phenylalanine ammonia-lyase has tyrosine ammonia-lyase activity". Plant Physiology. 113 (1): 175–9. doi:10.1104/pp.113.1.175. PMC 158128. PMID 9008393.

[2] Watts KT, Mijts BN, Lee PC, Manning AJ, Schmidt-Dannert C (December 2006). "Discovery of a substrate selectivity switch in tyrosine ammonia-lyase, a member of the aromatic amino acid lyase family". Chemistry & Biology. 13 (12): 1317–26. doi:10.1016/j.chembiol.2006.10.008. PMID 17185227.

[3] Louie GV, Bowman ME, Moffitt MC, Baiga TJ, Moore BS, Noel JP (December 2006). "Structural determinants and modulation of substrate specificity in phenylalanine-tyrosine ammonia-lyases". Chemistry & Biology. 13 (12): 1327–38. doi:10.1016/j.chembiol.2006.11.011. PMC 2859959. PMID 17185228.

[4] Schwede TF, Rétey J, Schulz GE (April 1999). "Crystal structure of histidine ammonia-lyase revealing a novel polypeptide modification as the catalytic electrophile". Biochemistry. 38 (17): 5355–61. doi:10.1021/bi982929q. PMID 10220322.

[5] Barros J, Serrani-Yarce JC, Chen F, Baxter D, Venables BJ, Dixon RA (May 2016). "Role of bifunctional ammonia-lyase in grass cell wall biosynthesis". Nature Plants. 2 (6): 16050. doi:10.1038/nplants.2016.50. PMID 27255834.

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@@ Line 1: / Line 1: @@
 {{Infobox enzyme
-| Name = Phenylalanine/tyrosine ammonia-lyase
+| Name       = Phenylalanine/tyrosine ammonia-lyase
-| EC_number = 4.3.1.25
+| EC_number  = 4.3.1.25
 | CAS_number =
+| GO_code    =
-| IUBMB_EC_number = 4/3/1/25
-| GO_code =
+| image      =
-| image =
+| width      =
-| width =
+| caption    =
-| caption =
 }}
-'''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 4.3.1.25, '''PTAL''', '''bifunctional PAL''') is an [[enzyme]] with [[List of enzymes|systematic name]] '''<small>L</small>-phenylalanine(or <small>L</small>-tyrosine):''trans''-cinnamate(or ''trans-p''-hydroxycinnamate) ammonia-lyase'''.<ref>{{cite journal | vauthors = Rösler J, Krekel F, Amrhein N, Schmid J | title = Maize phenylalanine ammonia-lyase has tyrosine ammonia-lyase activity | journal = Plant Physiology | volume = 113 | issue = 1 | pages = 175–9 | date = January 1997 | pmid = 9008393 | pmc = 158128 | doi = 10.1104/pp.113.1.175 }}</ref><ref>{{cite journal | vauthors = Watts KT, Mijts BN, Lee PC, Manning AJ, Schmidt-Dannert C | title = Discovery of a substrate selectivity switch in tyrosine ammonia-lyase, a member of the aromatic amino acid lyase family | journal = Chemistry & Biology | volume = 13 | issue = 12 | pages = 1317–26 | date = December 2006 | pmid = 17185227 | doi = 10.1016/j.chembiol.2006.10.008 | doi-access =  }}</ref><ref>{{cite journal | vauthors = Louie GV, Bowman ME, Moffitt MC, Baiga TJ, Moore BS, Noel JP | title = Structural determinants and modulation of substrate specificity in phenylalanine-tyrosine ammonia-lyases | journal = Chemistry & Biology | volume = 13 | issue = 12 | pages = 1327–38 | date = December 2006 | pmid = 17185228 | pmc = 2859959 | doi = 10.1016/j.chembiol.2006.11.011 }}</ref><ref>{{cite journal | vauthors = Schwede TF, Rétey J, Schulz GE | title = Crystal structure of histidine ammonia-lyase revealing a novel polypeptide modification as the catalytic electrophile | journal = Biochemistry | volume = 38 | issue = 17 | pages = 5355–61 | date = April 1999 | pmid = 10220322 | doi = 10.1021/bi982929q }}</ref><ref>{{cite journal | vauthors = Barros J, Serrani-Yarce JC, Chen F, Baxter D, Venables BJ, Dixon RA | title = Role of bifunctional ammonia-lyase in grass cell wall biosynthesis | journal = Nature Plants | volume = 2 | issue = 6 | pages = 16050 | date = May 2016 | pmid = 27255834 | doi = 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>
+: (1) <small>L</small>-[[phenylalanine]] <math>\rightleftharpoons</math> [[trans-cinnamate|''trans''-cinnamate]] + NH<sub>3</sub>
-: (2) L-[[tyrosine]] <math>\rightleftharpoons</math> trans-p-hydroxycinnamate + NH<sub>3</sub>
+: (2) <small>L</small>- [[tyrosine]] <math>\rightleftharpoons</math> ''trans-p''-hydroxycinnamate + NH<sub>3</sub>
 This enzyme is a member of the aromatic amino acid lyase family.
@@ Line 24: / Line 23: @@
 {{Carbon-nitrogen lyases}}
 {{Enzymes}}
-{{Portal bar|Molecular and Cellular Biology|border=no}}
+{{Portal bar|Biology|border=no}}
 {{DEFAULTSORT:Phenylalanine tyrosine ammonia-lyase}}

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)