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Ligand L-m-Tyr

Basic Ligand Information

Molecular Structure

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Roles as Enzyme Ligand

In Vivo Product in Enzyme-catalyzed Reactions (1 result)

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Show Natural Product (1 entry)

EC NUMBER

PROVEN IN VIVO REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

1.14.16.7

L-phenylalanine + tetrahydrobiopterin + O2 = 3-hydroxy-L-phenylalanine + 4a-hydroxytetrahydrobiopterin

-

-

Substrate in Enzyme-catalyzed Reactions (8 results)

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Show Substrate (8 entries)

EC NUMBER

REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

2.5.1.34

dimethylallyl diphosphate + L-m-tyrosine = diphosphate + 4-(3-methylbut-2-enyl)-L-m-tyrosine + 6-(3-methylbut-2-enyl)-L-m-tyrosine

739221

-

4.1.1.28

m-Tyr = ?

4210, 4213, 4207, 4218

-

4.1.99.2

L-m-Tyr + pyridoxal phosphate = pyridoxamine phosphate + keto acid

33443

-

4.3.1.24

(2S)-2-amino-3-(3-hydroxyphenyl)propanoic acid = (2E)-3-(3-hydroxyphenyl)prop-2-enoic acid + NH3

729395

-

6.1.1.20

ATP + 3-L-tyrosine + tRNAPhe = AMP + diphosphate + 3-L--tyrosyl-tRNAPhe

744547

3hfv, 3D-view

6.1.1.20

ATP + 3-L-tyrosine + tRNAPhe = AMP + diphosphate + 3-L--tyrosyl-tRNAPhe

744547

3hfz, 3D-view

6.1.1.20

ATP + 3-L-tyrosine + tRNAPhe = AMP + diphosphate + 3-L-tyrosyl-tRNAPhe

745346

3hfv, 3D-view

6.1.1.20

ATP + 3-L-tyrosine + tRNAPhe = AMP + diphosphate + 3-L-tyrosyl-tRNAPhe

745346

3hfz, 3D-view

6.1.1.20

4 entries

Product in Enzyme-catalyzed Reactions (4 results)

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Show Product (4 entries)

EC NUMBER

REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

1.14.16.7

L-phenylalanine + 6-methyltetrahydropterin + O2 = 3-hydroxy-L-phenylalanine + 4a-hydroxy-6-methyltetrahydropterin

-

-

1.14.16.7

L-phenylalanine + tetrahydrobiopterin + O2 = 3-hydroxy-L-phenylalanine + 4a-hydroxytetrahydrobiopterin

-

-

1.14.16.7

2 entries

4.3.1.24

3-hydroxy-trans-cinnamate + NH3 = 3-hydroxy-L-phenylalanine

-

-

4.3.1.25

3-hydroxy-trans-cinnamate + NH3 = 3-hydroxy-L-phenylalanine

-

-

Inhibitor in Enzyme-catalyzed Reactions (3 results)

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Show Inhibitors (3 entries)

EC NUMBER

COMMENTARY

LITERATURE

ENZYME 3D STRUCTURE

2.5.1.54

-

639750

-

4.1.99.2

competitive

33443, 33451

-

4.2.1.51

-

33886

-

3D Structure of Enzyme-Ligand-Complex (PDB) (16 results)

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Show 3D Structure of Enzyme-Ligand-Complex (PDB) (16 entries)

EC NUMBER

ENZYME 3D STRUCTURE

1.14.16.2

2toh, 3D-view

1.17.4.1

1biq, 3D-view

6.1.1.20

3hfv, 3D-view

6.1.1.20

3hfz, 3D-view

6.1.1.20

3hfv, 3D-view

6.1.1.20

3hfz, 3D-view

6.1.1.20

3hfv, 3D-view

6.1.1.20

3hfz, 3D-view

6.1.1.20

3hfv, 3D-view

6.1.1.20

3hfz, 3D-view

6.1.1.20

3hfv, 3D-view

6.1.1.20

3hfz, 3D-view

6.1.1.20

3hfv, 3D-view

6.1.1.20

3hfz, 3D-view

6.1.1.20

3hfv, 3D-view

6.1.1.20

3hfz, 3D-view

6.1.1.20

14 entries

Enzyme Kinetic Parameters

k_cat Value (Turnover Number) (4 results)

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Show Turnover Number (4 entries)

EC NUMBER

TURNOVER NUMBER [1/S]

TURNOVER NUMBER MAXIMUM [1/S]

COMMENTARY

LITERATURE

2.5.1.34

0.0065

-

pH 7.5, 37°C, recombinant enzyme

739221

4.1.99.2

0.00268

-

transamination

33443

4.3.1.24

0.89

-

pH 8.3, 30°C

729395

6.1.1.20

26

-

at pH 7.5 and 37°C

745346

K_M Value (5 results)

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Show KM Value (5 entries)

EC NUMBER

KM VALUE [MM]

KM VALUE MAXIMUM [MM]

COMMENTARY

LITERATURE

2.5.1.34

0.9

-

pH 7.5, 37°C, recombinant enzyme

739221

4.1.1.28

0.52

-

-

4218

4.1.99.2

0.94

-

transamination

33443

4.3.1.24

1.11

-

pH 8.3, 30°C

729395

6.1.1.20

1.15

-

at pH 7.5 and 37°C

745346

References & Links

Literature References (12)

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Show Reference (12 entries)

BRENDA REFERENCE ID

PUBMED ID

TITLE

YEAR

AUTHORS

JOURNAL

VOLUME

PAGES

4207

3533158

Aromatic-L-amino-acid decarboxylase activity in mouse pancreatic islets

1986

Lindström, P.

Biochim. Biophys. Acta

884

276-281

4210

-

Aromatic L-amino acid decarboxylase (guinea pig kidney)

1971

Lovenberg, W.

Methods Enzymol.

17B

652-656

4213

309771

Substrate specificity and other properties of dopa decarboxylase from guinea pig kidneys

1978

Srinivasan, K.; Awapara, J.

Biochim. Biophys. Acta

526

597-604

4218

3600369

Aromatic-L-amino acid decarboxylase from pig kidney

1987

Voltattorni, C.B.; Giartosio, A.; Turano, C.

Methods Enzymol.

142

179-187

33443

3691524

Transamination catalysed by tyrosine phenol-lyase from Citrobacter intermedius

1987

Demidkina, T.V.; Myagkikh, I.V.; Azhayev, A.V.

Eur. J. Biochem.

170

311-316

33451

721797

Elementary processes in the interaction of tyrosine phenol lyase with inhibitors and substrate

1978

Muro, T.; Nakatani, H.; Hiromi, K.; Kumagai, H.; Yamada, H.

J. Biochem.

84

633-640

33886

4261395

Chorismate mutase-prephenate dehydratase from Escherichia coli K-12. II. Kinetic properties

1972

Dopheide, T.A.A.; Crewther, P.; Davidson, B.E.

J. Biol. Chem.

247

4447-4452

639750

12953

Studies on 3-deoxy-D-arabinoheptulosonate-7-phosphate synthetase(phe) from Escherichia coli K12. 3. Structural studies

1976

Simpson, R.J.; Davidson, B.E.

Eur. J. Biochem.

70

509-516

729395

25037641

Bacterial Anabaena variabilis phenylalanine ammonia lyase: A biocatalyst with broad substrate specificity

2014

Lovelock, S.; Turner, N.

Bioorg. Med. Chem.

22

5555-5557

739221

26077893

Tryptophan prenyltransferases showing higher catalytic activities for Friedel-Crafts alkylation of o- and m-tyrosines than tyrosine prenyltransferases

2015

Fan, A.; Xie, X.; Li, S.M.

Org. Biomol. Chem.

13

7551-7557

744547

25545851

Molecular polygamy The promiscuity of L-phenylalanyl-tRNA-synthetase triggers misincorporation of meta- and ortho-tyrosine in monoclonal antibodies expressed by Chinese hamster ovary cells

2015

Popp, O.; Larraillet, V.; Kettenberger, H.; Gorr, I.H.; Hilger, M.; Lipsmeier, F.; Zeck, A.; Beaucamp, N.

Biotechnol. Bioeng.

112

1187-1199

745346

27226603

Multiple quality control pathways limit non-protein amino acid use by yeast cytoplasmic phenylalanyl-tRNA synthetase

2016

Moghal, A.; Hwang, L.; Faull, K.; Ibba, M.

J. Biol. Chem.

291

15796-15805

Links to other databases for L-m-Tyr

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Show Links (1 entry)

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PubChem