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Ligand alkylamine

Basic Ligand Information

Molecular Structure

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Roles as Enzyme Ligand

In Vivo Substrate in Enzyme-catalyzed Reactions (26 results)

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Show Natural Substrate (26 entries)

EC NUMBER

PROVEN IN VIVO REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

1.4.3.21

RCH2NH2 + H2O + O2 = RCHO + NH3 + H2O2

724323, 724280

-

1.4.3.22

RCH2NH2 + H2O + O2 = RCHO + NH3 + H2O2

391922

-

1.4.3.4

RCH2NH2 + H2O + O2 = RCHO + NH3 + H2O2

394572, 394575, 394556, 394574, 394551, 394583, 394568, 394588, 394573

-

2.3.2.13

alpha-casein glutamine + alkylamine = alpha-casein N5-alkylglutamine + NH3

759558

-

2.3.2.13

alpha-synuclein glutamine + alkylamine = alpha-synuclein N5-alkylglutamine + NH3

759712

-

2.3.2.13

ApoE glutamine + alkylamine = ApoE N5-alkylglutamine + NH3

759712

-

2.3.2.13

beta-crystallin glutamine + alkylamine = beta-crystallin N5-alkylglutamine + NH3

758635

-

2.3.2.13

casein glutamine + alkylamine = casein N5-alkylglutamine + NH3

759197

-

2.3.2.13

Cbz-Gln-Gly + alkylamine = Cbz-Glu-Gly + NH3

736618

-

2.3.2.13

Cbz-L-Gln-Gly + alkylamine = ?

719054

-

2.3.2.13

collagen glutamine + alkylamine = collagen N5-alkylglutamine + NH3

759197

-

2.3.2.13

fibronectin-bound gamma-glutamine + alkylamine = fibronectin N5-alkylglutamine + NH3

720010

-

2.3.2.13

fibronectinglutamine + alkylamine = fibronectin N5-alkylglutamine + NH3

758635

-

2.3.2.13

gelatin glutamine + alkylamine = gelatin N5-alkylglutamine + NH3

759197

-

2.3.2.13

gliadin glutamine + alkylamine = gliadin N5-alkylglutamine + NH3

759712

-

2.3.2.13

leishmanolysin + alkylamine = ?

673490

-

2.3.2.13

myo-inositol-1-phosphate synthase + alkylamine = ?

673490

-

2.3.2.13

N-acetyl-PNPQLPF + alkylamine = ?

720978

-

2.3.2.13

N-carboxybenzoyl-L-glutaminylglycine + alkylamine = ?

720112

-

2.3.2.13

N-Cbz-L-glutaminyl(gamma-4-nitrophenylester)glycine + alkylamine = ?

720978

-

2.3.2.13

plugin glutamine + alkylamine = plugin N5-alkylglutamine + NH3

736440

-

2.3.2.13

protein glutamine + alkylamine = protein N5-alkylglutamine + NH3

759603, 758664, 759214, 759675, 758566, 759212, 758635, 758700, 758750, 759154, 759166, 759606, 759712, 760040, 758632, 758686, 758740, 758870, 758871, 758939, 758966, 759558, 759632, 760096, 759209, 759049, 759631, 758724, 758981, 759197, 759274, 758965, 759482, 759518, 759529

-

2.3.2.13

protein-bound gamma-glutamine + alkylamine = protein N5-alkylglutamine + NH3

718945, 487865, 487835, 487851, 487850, 487857, 487831, 487826, 487833, 487820, 487868

-

2.3.2.13

transforming growth factor-beta glutamine + alkylamine = transforming growth factor-beta N5-alkylglutamine + NH3

758635

-

2.3.2.13

[amyloid-beta]-L-glutamine + alkylamine = [amyloid-beta]-N5-alkyl-L-glutamine + NH3

737260

-

2.3.2.13

[protein]-L-glutamine + alkylamine = [protein]-N5-alkyl-L-glutamine + NH3

737135, 735685, 736082, 736442, 735910, 736069, 737130, 736699, 735501, 735541, 737209, 720978, 735632, 737093, 735731, 735846, 735847

-

2.3.2.13

23 entries

Substrate in Enzyme-catalyzed Reactions (48 results)

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Show Substrate (48 entries)

EC NUMBER

REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

1.4.3.13

n-alkylamine + O2 + H2O = aldehyde + NH3 + H2O2

659558

-

1.4.3.21

RCH2NH2 + H2O + O2 = RCHO + NH3 + H2O2

391910, 391914, 391915, 391916, 391932, 391937, 391908, 724323, 391949, 391956, 391960, 724280

-

1.4.3.22

RCH2NH2 + H2O + O2 = RCHO + NH3 + H2O2

391940, 391941, 391922, 209612, 391931, 391947, 391909, 391911, 391917, 391918, 391920, 391933, 391934, 391955, 391952, 391953, 391912, 391913, 391928, 391944, 391948, 391958, 391942, 391950, 391926, 391945, 391954, 391927, 391951, 391919, 391935, 391923, 391943, 391925, 391959

-

1.4.3.4

RCH2NH2 + H2O + O2 = RCHO + NH3 + H2O2

394552, 394553, 394555, 394560, 394564, 394568, 394572, 394575, 394556, 394558, 394567, 394587, 394570, 394563, 394576, 394583, 394562, 394574, 394548, 394573, 394549, 394557, 391951, 394559, 394569, 394565, 394566, 394579, 394582, 394580, 394561, 394577, 394551, 394588

-

1.4.9.1

RCH2NH2 + acceptor + H2O = RCHO + NH3 + reduced acceptor

396582, 396581, 396571, 396572, 396574, 396577, 396576, 396585, 396583

-

2.3.2.13

Ac-PNPQLPF-OH + alkylamine = ?

720978

-

2.3.2.13

alpha-casein glutamine + alkylamine = alpha-casein N5-alkylglutamine + NH3

759558

-

2.3.2.13

alpha-synuclein glutamine + alkylamine = alpha-synuclein N5-alkylglutamine + NH3

759712

-

2.3.2.13

ApoE glutamine + alkylamine = ApoE N5-alkylglutamine + NH3

759712

-

2.3.2.13

beta-crystallin glutamine + alkylamine = beta-crystallin N5-alkylglutamine + NH3

758635

-

2.3.2.13

biotinyl-Aca-DDWDAMDEQIWF + alkylamine = ?

758981

-

2.3.2.13

biotinyl-HQSYVDPWMLDH + alkylamine = ?

758981

-

2.3.2.13

bovine serum albumin glutamine + alkylamine = bovine serum albumin N5-alkylglutamine + NH3

759529

-

2.3.2.13

casein glutamine + alkylamine = casein N5-alkylglutamine + NH3

759197, 759529

-

2.3.2.13

Cbz-Gln-Gly + alkylamine = ?

735930

-

2.3.2.13

Cbz-Gln-Gly + alkylamine = Cbz-Glu-Gly + NH3

736618

-

2.3.2.13

Cbz-L-Gln-Gly + alkylamine = ?

719054

-

2.3.2.13

collagen glutamine + alkylamine = collagen N5-alkylglutamine + NH3

759197

-

2.3.2.13

fibronectin-bound gamma-glutamine + alkylamine = fibronectin N5-alkylglutamine + NH3

720010

-

2.3.2.13

fibronectinglutamine + alkylamine = fibronectin N5-alkylglutamine + NH3

758635

-

2.3.2.13

gelatin glutamine + alkylamine = gelatin N5-alkylglutamine + NH3

759212, 759197

-

2.3.2.13

gliadin glutamine + alkylamine = gliadin N5-alkylglutamine + NH3

759712

-

2.3.2.13

leishmanolysin + alkylamine = ?

673490

-

2.3.2.13

myo-inositol-1-phosphate synthase + alkylamine = ?

673490

-

2.3.2.13

N-acetyl-PNPQLPF + alkylamine = ?

720978

-

2.3.2.13

N-carboxybenzoyl-L-glutaminylglycine + alkylamine = ?

720112

-

2.3.2.13

N-Cbz-Gln-Gly + alkylamine = ? + NH3

735846

-

2.3.2.13

N-Cbz-Glu(gamma-4-nitrophenylester)Gly + alkylamine = 4-nitrophenol + ?

720978

-

2.3.2.13

N-Cbz-L-glutaminyl(gamma-4-nitrophenylester)glycine + alkylamine = ?

720978

-

2.3.2.13

Nalpha-benzyloxycarbonyl-L-Gln-Gly + alkylamine = ?

719877

-

2.3.2.13

plugin glutamine + alkylamine = plugin N5-alkylglutamine + NH3

736440

-

2.3.2.13

protein glutamine + alkylamine = protein N5-alkylglutamine + NH3

759603, 758664, 759214, 759675, 758566, 759212, 758635, 758700, 758750, 759154, 759166, 759606, 759712, 760040, 758632, 758686, 758740, 758870, 758871, 758939, 758966, 759558, 759632, 760096, 759209, 759049, 759631, 758724, 758981, 759197, 759274, 758965, 759482, 759518, 759529

-

2.3.2.13

protein-bound gamma-glutamine + alkylamine = protein N5-alkylglutamine + NH3

487822, 487845, 487856, 487867, 487872, 487878, 487861, 487868, 718945, 487823, 487858, 487853, 487875, 487871, 487825, 487820, 487854, 487876, 487827, 487863, 487833, 487843, 487828, 487834, 487830, 487826, 487865, 487835, 487851, 487850, 487857, 487831

-

2.3.2.13

transforming growth factor-beta glutamine + alkylamine = transforming growth factor-beta N5-alkylglutamine + NH3

758635

-

2.3.2.13

TVQQEL + alkylamine = ?

736440

-

2.3.2.13

YENHKLPSSWPF + alkylamine = Y-N5-alkylglutaminyl-NHKLPSSWPF + NH3

758724

-

2.3.2.13

Z-Gln-Gly + alkylamine = ?

737209

-

2.3.2.13

Z-Glu(HC)-Gly-OH + alkylamine = ?

759049

-

2.3.2.13

Z-Glu(HMC)-Gly-OH + alkylamine = ?

759049

-

2.3.2.13

Z-Glu(HMC)-OH + alkylamine = ?

759049

-

2.3.2.13

Z-Phe-gamma-Abu-7-hydroxy-4-methylcoumarin + alkylamine = Z-Phe-gamma-amino-N-alkylbutanamide + 7-hydroxy-4-methylcoumarin

759049

-

2.3.2.13

Z-Phe-gamma-Abu-7-hydroxycoumarin + alkylamine = Z-Phe-gamma-amino-N-alkylbutanamide + 7-hydroxycoumarin

759049

-

2.3.2.13

Z-Phe-Glu(HC)-Gly-OH + alkylamine = ?

759049

-

2.3.2.13

Z-Phe-Glu(HMC)-Gly-OH + alkylamine = ?

759049

-

2.3.2.13

Z-Phe-Glu(HMC)-OH + alkylamine = ?

759049

-

2.3.2.13

[amyloid-beta]-L-glutamine + alkylamine = [amyloid-beta]-N5-alkyl-L-glutamine + NH3

737260

-

2.3.2.13

[casein]-L-glutamine + alkylamine = [casein]-N5-alkyl-L-glutamine + NH3

735731

-

2.3.2.13

[protein]-L-glutamine + alkylamine = [protein]-N5-alkyl-L-glutamine + NH3

737135, 735685, 736082, 736442, 735910, 736069, 737130, 736699, 735501, 735541, 737209, 720978, 735632, 737093, 735731, 735846, 735847

-

2.3.2.13

43 entries

Activator in Enzyme-catalyzed Reactions (1 result)

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Show Activating Compound (1 entry)

EC NUMBER

COMMENTARY

LITERATURE

ENZYME 3D STRUCTURE

1.13.12.2

low concentrations stimulate lysine oxygenation

440267

-

Inhibitor in Enzyme-catalyzed Reactions (5 results)

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Show Inhibitors (5 entries)

EC NUMBER

COMMENTARY

LITERATURE

ENZYME 3D STRUCTURE

1.13.12.2

high concentration inhibits, low concentrations stimulate lysine oxygenation

440267

-

2.7.11.18

long and straight chain, most effective with chain length C-13 to C-18

640644

-

3.2.1.45

-

136458

-

3.4.21.50

-

36618

-

4.3.1.18

inactivation via a transimination of pyridoxal 5'-phosphate

210805

-

Enzyme Kinetic Parameters

References & Links

Literature References (188)

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Show Reference (188 entries)

BRENDA REFERENCE ID

PUBMED ID

TITLE

YEAR

AUTHORS

JOURNAL

VOLUME

PAGES

36618

7845202

Lysyl endopeptidase of Achromobacter lyticus

1994

Sakiyama, F.; Masaki, T.

Methods Enzymol.

244

126-137

136458

2956992

Human acid beta-glucosidase: use of inhibitors, alternative substrates and amphiphiles to investigate the properties of the normal and Gaucher disease active sites

1987

Osiecki-Newman, K.; Fabbro, D.; Legler, G.; Desnick, R.J.; Grabowski, G.A.

Biochim. Biophys. Acta

915

87-100

209612

409634

The purification and preliminary investigation of fumarase, peroxidase, diamine oxidase and adenosine deaminase from human seminal plasma

1977

Crabbe, M.J.; Kavanagh, J.P.

Biochem. Soc. Trans.

5

735-737

210805

7019208

Inactivation of D-serine dehydratase by alkylamines via a transimination of enzyme-linked cofactor

1981

Federiuk, C.S.; Shafer, J.A.

J. Biol. Chem.

256

7416-7423

391908

14002223

Monoamine oxidase II. Copper, one of the prosthetic groups of plasma monamine oxidase

1962

Yamada, H.; Yasunobu, K.T.

J. Biol. Chem.

237

3077-3082

391909

4964016

Pyridoxal phosphate as a prosthetic group of pig kidney diamine oxidase

1967

Mondovi, B.; Costa, M.T.; Agro, A.F.; Rotilio, G.

Arch. Biochem. Biophys.

119

373-381

391910

-

Pig liver monoamine oxidase I: isolation and characterization

1974

Carper, W.R.; Stoddard, D.D.; Martin, D.F.

Biochim. Biophys. Acta

334

287-296

391911

826412

Purification of pig kidney diamine oxidase by gel-exclusion chromatography

1976

Floris, G.; Fadda, M.B.; Pellegrini, M.; Corda, M.; Agro, A.F.

FEBS Lett.

72

179-181

391912

-

Purification and properties of pea cotyledon and embryo diamine oxidase

1977

Srivastava, S.K.; Prakash, V.

Phytochemistry

16

189-190

391913

4218929

Kinetic and other characteristics of diamine oxidase of pea seedlings

1974

Nylen, U.; Szybek, P.

Acta Chem. Scand. B

28

1153-1160

391914

6615797

Heterogeneity of pig plasma amine oxidase: molecular and catalytic properties of chromatographically isolated forms

1983

Falk, M.C.; Staton, A.J.; Williams, T.J.

Biochemistry

22

3746-3751

391915

4375031

Effect of azide on some spectral and kinetic properties of pig-plasma benzylamine oxidase

1974

Lindström, A.; Olsson, B.; Petterson, G.

Eur. J. Biochem.

48

237-243

391916

4364395

Kinetics of the interaction between pig-plasma benzylamine oxidase and hydrazine derivatives

1974

Lindström, A.; Olsson, B.; Petterson, G.

Eur. J. Biochem.

42

177-182

391917

4198360

Kinetics of the diamine oxidase reaction

1973

Bardsley, W.G.; Crabbe, M.J.C.; Shindler, J.S.

Biochem. J.

131

459-469

391918

5000447

On the active site of diamine oxidase: kinetic studies

1971

Costa, M.T.; Rotilio, G.; Agro, A.F.; Vallogini, M.P.; Mondovi, B.

Arch. Biochem. Biophys.

147

8-13

391919

11945979

Modification of catalytic properties of amine oxidases

1971

Stesina, L.N.; Akopyan, Z.I.; Gorkin, V.Z.

FEBS Lett.

16

349-351

391920

2503012

Characterization of free and immobilized amine oxidases

1989

Stevanato, R.; Porchia, M.; Befani, O.; Mondovi, B.; Rigo, A.

Biotechnol. Appl. Biochem.

11

266-272

391922

6403048

Distribution and properties of human intestinal diamine oxidase and its relevance for the histamine catabolism

1983

Bieganski, T.; Kusche, J.; Lorenz, W.; Hesterberg, R.; Stahlknecht, C.D.; Feussner, K.D.

Biochim. Biophys. Acta

756

196-203

391923

808238

Purification of histaminase (diamine oxidase) from human pregnancy plasma by affinity chromatography

1975

Baylin, S.B.; Margolis, S.

Biochim. Biophys. Acta

397

294-306

391925

-

Diamine oxidase from Lens esculenta seedlings: purification and properties

1983

Floris, G.; Giartosio, A.; Rinaldi, A.

Phytochemistry

22

1871-1874

391926

-

Purification and characterization of diamine oxidase from rice embryos

1984

Chaudhuri, M.M.; Ghosh, B.

Phytochemistry

23

241-243

391927

-

Purification and characterization of diamine oxidase from clover leaves

1987

Delhaize, E.; Webb, J.

Phytochemistry

26

641-643

391928

-

Purification and properties of diamine oxidase from pea epicotyls

1981

Yanagisawa, H.; Hirasawa, E.; Suzuki, Y.

Phytochemistry

20

2105-2108

391931

182134

Human placental diamine oxidase. Improved purification and characterization of a copper- and manganese-containing amine oxidase with novel substrate specificity

1976

Crabbe, M.J.C.; Waight, R.D.; Bardsley, W.G.; Barker, R.W.; Kelly, I.D.; Knowles, P.F.

Biochem. J.

155

679-687

391932

218560

Properties of cupric ions in benzylamine oxidase from pig plasma as studied by magnetic-resonance and kinetic methods

1979

Barker, R.; Boden, N.; Cayley, G.; Charlton, S.C.; Henson, R.; Holmes, M.C.; Kelly, I.D.; Knowles, P.F.

Biochem. J.

177

289-302

391933

2498301

Kinetic studies on the inhibition mechanism of diamine oxidase from porcine kidney by aminoguanidine

1989

Tamura, H.; Horiike, K.; Fukuda, H.; Watanabe, T.

J. Biochem.

105

299-306

391934

6403525

Spectroscopic and kinetics studies of the inhibition of pig kidney diamine oxidase by anions

1983

Dooley, D.M.; Golnik, K.C.

J. Biol. Chem.

258

4245-4248

391935

6814913

Purification and properties of diamine oxidase from Euphorbia latex

1982

Rinaldi, A.; Floris, G.; Finazzi-Agro, A.

Eur. J. Biochem.

127

417-422

391937

2848544

Purification of benzylamine oxidase from cultured porcine aortic smooth muscle cells

1988

Hysmith, R.M.; Boor, P.J.

Biochem. Cell Biol.

66

821-829

391940

2798365

Amine oxidase from Lathyrus cicera and Phaseolus vulgaris: purification and properties

1989

Cogoni, A.; Farci, R.; Medda, R.; Rinaldi, A.; Floris, G.

Prep. Biochem.

19

95-112

391941

-

Purification and properties of the diamine oxidase from Vicia faba leaves

1981

Matsuda, H.; Suzuki, Y.

Plant Cell Physiol.

22

737-746

391942

-

Partial purification and characterization of diamine oxidase from groundnut embryo

1980

Sindhu, R.K.; Desai, H.V.

Indian J. Biochem. Biophys.

17

194-197

391943

-

Diamine oxidase from sainfon (Onobrychis viciifolia). Purification and some properties

1989

Pec, P.; Zajoncova, L.; Jilek, M.

Biologia (Bratisl. )

44

1177-1184

391944

-

Purification and properties of diamine oxidase from soybean (Glycine max)

1989

Kang, J.H.; Cho, Y.D.

Hanguk Saenghwahakhoe Chi

22

361-366

391945

-

Lentil seedlings amine oxidase: preparation and properties of the copper-free enzyme

1986

Matsumiya, M.; Otake, S.

Nippon Suisan Gakkaishi

52

1617-1623

391947

-

Purification and properties of diamine oxidase from human kidney

1987

Suzuki, O.; Matsumoto, T.

Biogenic Amines

4

237-245

391948

8239662

Purification and characterization of amine oxidase from soybean seedlings

1993

Vianello, F.; Di Paolo, M.L.; Stevanato, R.; Gasparini, R.; Rigo, A.

Arch. Biochem. Biophys.

307

35-39

391949

8011631

Copper amine oxidase: heterologous expression, purification, and characterization of an active enzyme in Saccharomyces cerevisiae

1994

Cai, D.; Klinman, J.P.

Biochemistry

33

7647-7653

391950

8845363

The reaction mechanism of copper amine oxidase: detection of intermediates by the use of substrates and inhibitors

1995

Medda, R.; Padiglia, A.; Pedersen, J.Z.; Rotilio, G.; Agro, A.F.; Floris, G.

Biochemistry

34

16375-16381

391951

7727530

Amine oxidases from Aspergillus niger: identification of a novel flavin-dependent enzyme

1995

Schilling, B.; Lerch, K.

Biochim. Biophys. Acta

1243

529-537

391952

-

Purification and characterization of diamine oxidase from Triticum aestivum shoots

1996

Suzuki, Y.

Phytochemistry

42

291-293

391953

8620882

Two distinct quinoprotein amine oxidases are induced by n-butylamine in the mycelia of Aspergillus niger AKU 3302. Purification, characterization, cDNA cloning and sequencing

1996

Frebort, I.; Tamaki, H.; Ishida, H.; Pec, P.; Luhova, L.; Tsuno, H.; Halata, M.; Asano, Y.; Kato, Y.; et al.

Eur. J. Biochem.

237

255-265

391954

-

Quinoprotein amine oxidase from sainfoin seedlings

1997

Zajoncova, L.; Sebela, M.; Frebort, I.; Faulhammer, H.G.; Navratil, M.; Pec, P.

Phytochemistry

45

239-242

391955

9367901

Competitive inhibition of swine kidney copper amine oxidase by drugs: amiloride, clonidine, and gabexate mesylate

1997

Federico, R.; Angelini, R.; Ercolini, L.; Venturini, G.; Mattevi, A.; Ascenzi, P.

Biochem. Biophys. Res. Commun.

240

150-152

391956

9551552

Copper amine oxidase from Hansenula polymorpha: the crystal structure determined at 2.4 A resolution reveals the active conformation

1998

Li, R.; Klinman, J.P.; Mathews, F.S.

Structure

6

293-307

391958

9681017

Developmental expression and biochemical analysis of the Arabidopsis atao1 gene encoding an H2O2-generating diamine oxidase

1998

Moller, S.G.; McPherson, M.J.

Plant J.

13

781-791

391959

-

Analysis of the active sites of copper/topa quinone-containing amine oxidases from Lathyrus odoratus and L. sativus seedlings

1998

Sebela, M.; Luhova, L.; Frebort, I.; Faulhammer, H.G.; Hirota, S.; Zajoncova, L.; Stuzka, V.; Pec, P.

Phytochem. Anal.

9

211-222

391960

-

Evidence against reduction of Cu2+ to Cu+ during dioxygen activation in a copper amine oxidase from Yeast

2000

Mills, S.A.; Klinman, J.P.

J. Am. Chem. Soc.

122

9897-9904

394548

6061707

Mitochondrial monoamine oxidase. I. Purification and characterization of the bovine kidney enzyme

1967

Erwin, V.G.; Hellerman, L.

J. Biol. Chem.

242

4230-4238

394549

5657868

The prosthetic groups of pig brain mitochondrial monoamine oxidase

1968

Tipton, K.F.

Biochim. Biophys. Acta

159

451-459

394551

11049757

High-level expression of human liver monoamine oxidase B in Pichia pastoris

2000

Newton-Vinson, P.; Hubalek, F.; Edmondson, D.E.

Protein Expr. Purif.

20

334-345

394552

11812236

High-level expression of human liver monoamine oxidase A in Pichia pastoris: comparison with the enzyme expressed in Saccharomyces cerevisiae

2002

Li, M.; Hubalek, F.; Newton-Vinson, P.; Edmondson, D.E.

Protein Expr. Purif.

24

152-162

394553

11732903

Loss of serotonin oxidation as a component of the altered substrate specificity in the Y444F mutant of recombinant human liver MAO A

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Nandigama, R.K.; Miller, J.R.; Edmondson, D.E.

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Boehme, B.; Moritz, B.; Wendler, J.; Hertel, T.C.; Ihling, C.; Brandt, W.; Pietzsch, M.

Amino Acids

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Substrates, inhibitors, and probes of mammalian transglutaminase 2

2020

Zhuang, R.; Khosla, C.

Anal. Biochem.

591

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Purification of bovine liver transglutaminase by gel filtration

2020

Razavian, S.; Kashfi, A.; Khoshraftar, Z.

Appl. Biol. Chem.

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Bioengineering of microbial transglutaminase for biomedical applications

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Chan, S.K.; Lim, T.S.

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15(V/K) kinetic isotope effect and steady-state kinetic analysis for the transglutaminase 2 catalyzed deamidation and transamidation reactions

2018

Wells, E.A.; Anderson, M.A.; Zeczycki, T.N.

Arch. Biochem. Biophys.

643

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Analysis on transglutaminase 1 and its substrates using specific substrate peptide in cultured keratinocytes

2016

Yamane, M.; Sugimura, K.; Kawasaki, H.; Tatsukawa, H.; Hitomi, K.

Biochem. Biophys. Res. Commun.

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Enhancing the activity and thermostability of Streptomyces mobaraensis transglutaminase by directed evolution and molecular dynamics simulation

2019

Liu, Y.; Huang, L.; Shan, M.; Sang, J.; Li, Y.; Jia, L.; Wang, N.; Wang, S.; Shao, S.; Liu, F.; Lu, F.

Biochem. Eng. J.

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Identification of DNAJA1 as a novel interacting partner and a substrate of human transglutaminase 2

2016

Erguelen, E.; Becsi, B.; Csomos, I.; Fesues, L.; Kanchan, K.

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Site-specific conjugation to native and engineered lysines in human immunoglobulins by microbial transglutaminase

2017

Spidel, J.L.; Vaessen, B.; Albone, E.F.; Cheng, X.; Verdi, A.; Kline, J.B.

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2019

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Molecular insights into the mechanism of substrate recognition of Streptomyces transglutaminases

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Improving the active expression of transglutaminase in Streptomyces lividans by promoter engineering and codon optimization

2016

Liu, S.; Wang, M.; Du, G.; Chen, J.

BMC Biotechnol.

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Constitutive expression of active microbial transglutaminase in Escherichia coli and comparative characterization to a known variant

2017

Javitt, G.; Ben-Barak-Zelas, Z.; Jerabek-Willemsen, M.; Fishman, A.

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In situ enzymatic activity of transglutaminase isoforms on brain tissue sections of rodents A new approach to monitor differences in post-translational protein modifications during neurodegeneration

2016

Schulze-Krebs, A.; Canneva, F.; Schnepf, R.; Dobner, J.; Dieterich, W.; Von Hoersten, S.

Brain Res.

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Synthesis and kinetic characterisation of water-soluble fluorogenic acyl donors for transglutaminase 2

2016

Wodtke, R.; Schramm, G.; Pietzsch, J.; Pietsch, M.; Loeser, R.

ChemBioChem

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Tissue transglutaminase activity in human gastric mucosa according to Helicobacter pylori infection

2018

Pina Dore, M.; Pes, G.M.; Errigo, A.; Manca, A.; Realdi, G.

Exp. Biol. Med. (Maywood)

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Characterisation of a novel cold-adapted calcium-activated transglutaminase implications for medicine and food processing

2020

Alvarez, R.G.; Karki, P.; Langleite, I.E.; Bakksjo, R.J.; Eichacker, L.A.; Furnes, C.

FEBS Open Bio

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Characterization of a cold-active transglutaminase from a crayfish, Pacifastacus leniusculus

2018

Sirikharin, R.; Soederhaell, I.; Soederhaell, K.

Fish Shellfish Immunol.

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A cold active transglutaminase from Antarctic krill (Euphausia superba) purification, characterization and application in the modification of cold-set gelatin gel

2017

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232

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Optimization of recombinant Zea mays transglutaminase production and its influence on the functional properties of yogurt

2017

Li, H.; Cui, Y.; Zhang, L.; Zhang, L.; Liu, H.; Yu, J.

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The over-expression of the plastidial transglutaminase from maize in Arabidopsis increases the activation threshold of photoprotection

2016

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Discovery of a microbial transglutaminase enabling highly site-specific labeling of proteins

2017

Steffen, W.; Ko, F.C.; Patel, J.; Lyamichev, V.; Albert, T.J.; Benz, J.; Rudolph, M.G.; Bergmann, F.; Streidl, T.; Kratzsch, P.; Boenitz-Dulat, M.; Oelschlaegel, T.; Schraeml, M.

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2017

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Purification and biochemical characterization of a novel transglutaminase from Mythimna separata larvae (Noctuidae, Lepidoptera)

2018

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Microbial transglutaminase alters the immunogenic potential and cross-reactivity of horse and cow milk proteins

2020

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J. Dairy Sci.

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Structure-activity relationships of potent, targeted covalent inhibitors that abolish both the transamidation and GTP binding activities of human tissue transglutaminase

2017

Akbar, A.; McNeil, N.M.R.; Albert, M.R.; Ta, V.; Adhikary, G.; Bourgeois, K.; Eckert, R.L.; Keillor, J.W.

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Nepsilon-acryloyllysine piperazides as irreversible inhibitors of transglutaminase 2 synthesis, structure-activity relationships, and pharmacokinetic profiling

2018

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Specificity of transglutaminase-catalyzed peptide synthesis

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St-Jacques, A.; Rachel, N.; Curry, D.; Gillet, S.; Clouthier, C.; Keillor, J.; Pelletier, J.; Chica, R.

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Purification and characterization of a high-salt-resistant microbial transglutaminase from Streptomyces mobaraensis

2016

Jin, M.; Huang, J.; Pei, Z.; Huang, J.; Gao, H.; Chang, Z.

J. Mol. Catal. B

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Expression of Zea mays transglutaminase in Pichia pastoris under different promoters and its impact on properties of acidified milk protein concentrate gel

2019

Li, H.; Zhang, T.; Li, J.; Li, H.; Xu, Y.; Yu, J.

J. Sci. Food Agric.

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Opening up about tissue transglutaminase when conformation matters more than enzymatic activity

2018

Katt, W.P.; Antonyak, M.A.; Cerione, R.A.

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Structure of natural variant transglutaminase 2 reveals molecular basis of gaining stability and higher activity

2018

Ha, H.J.; Kwon, S.; Jeong, E.M.; Kim, C.M.; Lee, K.B.; Kim, I.G.; Park, H.H.

PLoS ONE

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Engineered, highly reactive substrates of microbial transglutaminase enable protein labeling within various secondary structure elements

2017

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Protein Sci.

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Links to other databases for alkylamine

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