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Ligand Gly-Gly

Basic Ligand Information

Molecular Structure

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Roles as Enzyme Ligand

In Vivo Product in Enzyme-catalyzed Reactions (2 results)

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Show Natural Product (2 entries)

EC NUMBER

PROVEN IN VIVO REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

3.4.22.B60

Z-Gly-Pro-Gly-Gly-Pro-Ala + H2O = Z-Gly-Pro + Gly-Gly + L-Pro-L-Ala

0

-

3.4.24.75

pentaglycine + H2O = diglycine + triglycine

0

-

Substrate in Enzyme-catalyzed Reactions (78 results)

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Show Substrate (78 entries)

EC NUMBER

REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

1.4.3.19

glycylglycine + H2O + O2 = ?

743136

-

2.1.4.2

streptidine phosphate + glycylglycine = ?

485964, 485981, 485984, 485989

-

2.3.2.2

5-L-glutamyl 4-nitroanilide + Gly-Gly = 4-nitroaniline + 5-L-glutamyl-Gly-Gly

689579

-

2.3.2.2

5-L-glutamyl-4-nitroanilide + Gly-Gly = 4-nitroaniline + 5-L-glutamyl-Gly-Gly

658567, 675471, 704637, 672838, 703332, 703335, 674593, 676991, 672686, 689061, 673912, 703990, 704335

-

2.3.2.2

5-L-glutamyl-L-His + Gly-Gly = L-His + 5-L-glutamyl-Gly-Gly

658567

-

2.3.2.2

5-L-glutamyl-L-Met + Gly-Gly = L-Met + 5-L-glutamyl-Gly-Gly

658567

-

2.3.2.2

5-L-glutamyl-L-Phe + Gly-Gly = L-Phe + 5-L-glutamyl-Gly-Gly

658567

-

2.3.2.2

5-L-glutamyl-L-Trp + Gly-Gly = L-Trp + 5-L-glutamyl-Gly-Gly

658567

-

2.3.2.2

5-L-glutamyl-L-Tyr + Gly-Gly = L-Tyr + 5-L-glutamyl-Gly-Gly

658567

-

2.3.2.2

5-L-glutamyl-L-Val + Gly-Gly = L-Val + 5-L-glutamyl-Gly-Gly

658567

-

2.3.2.2

D-Gln + Gly-Gly = Glu-Gly-Gly + NH3

657592

-

2.3.2.2

gamma-Glu-Cys + Gly-Gly = Cys + 5-L-glutamyl-Gly-Gly

672686

-

2.3.2.2

gamma-L-glutamyl-4-nitroanilide + Gly-Gly = 4-nitroaniline + gamma-L-glutamyl-Gly-Gly

727437

-

2.3.2.2

glutathione + Gly-Gly = L-cysteinylglycine + 5-L-glutamyl-Gly-Gly

672422

-

2.3.2.2

GS-bimane + Gly-Gly = ?

672686

-

2.3.2.2

GSH + Gly-Gly = ?

672686, 658567

-

2.3.2.2

GSSG + Gly-Gly = ?

672686

-

2.3.2.2

L-Gln + Gly-Gly = NH3 + 5-L-glutamyl-Gly-Gly

658567

-

2.3.2.2

5-L-glutamyl-4-nitroanilide + glycyl-glycine = 4-nitroaniline + 5-L-glutamyl-glycyl-glycine

686496

-

2.3.2.2

S-nitroso-glutathione + glycyl-glycine = S-nitroso-cysteinylglycine + gamma-L-glutamyl-glycyl-glycine

701909, 701918

-

2.3.2.2

(gamma-L-glutamyl)-4-nitroanilide + glycylglycine = 4-nitroaniline + gamma-glutamylglycylglycine

756547, 756619, 756753

-

2.3.2.2

1-menaphthylglutathione + glycylglycine = ?

735923

-

2.3.2.2

2,4-dinitrophenylglutathione + glycylglycine = ?

735923

-

2.3.2.2

4,4'-diphenylmethane diisocyanate linked (Cys-Gly)-GSH + glycylglycine = 4,4'-diphenylmethane diisocyanate linked (Cys-Gly)-(Cys-Gly) + L-Glu-Gly-Gly

737307

-

2.3.2.2

4,4'-diphenylmethane diisocyanate linked GSH-GSH + glycylglycine = 4,4'-diphenylmethane diisocyanate linked (Cys-Gly)-GSH + L-Glu-Gly-Gly

737307

-

2.3.2.2

4-methylbiphenylylglutathione + glycylglycine = ?

735923

-

2.3.2.2

4-nitrobenzylglutathione + glycylglycine = ?

735923

-

2.3.2.2

5-D-glutamyl 3-carboxy-4-nitroanilide + glycylglycine = 5-D-glutamyl-glycylglycine + 3-carboxy-4-nitroaniline

487934

-

2.3.2.2

5-L-glutamyl 3-carboxy-4-nitroanilide + glycylglycine = 5-L-glutamyl-glycylglycine + 3-carboxy-4-nitroaniline

487897, 487934

-

2.3.2.2

5-L-glutamyl 3-carboxy-4-nitronailide + glycylglycine = 5-amino-2-nitrobenzoic acid + 5-L-glutamylglycylglycine

487933, 487934

-

2.3.2.2

5-L-glutamyl-(3-carboxyl)-4-nitroanilide + glycylglycine = 3-carboxyl-4-nitroaniline + 5-L-glutamyl-glycylglycine

736144

-

2.3.2.2

5-L-glutamyl-2-naphthylamide + glycylglycine = 5-L-glutamyl-glycylglycine + 2-naphthylamine

718951

-

2.3.2.2

5-L-glutamyl-3-carboxy-4-nitroanilide + glycylglycine = 5-L-glutamyl-glycylglycine + 3-carboxy-4-nitroaniline

487897, 487932, 487933, 487934, 487921

-

2.3.2.2

5-L-glutamyl-4-methoxy-2-naphthylamide + glycylglycine = 5-L-glutamyl-glycylglycine + 4-methoxy-2-naphthylamine

720135

-

2.3.2.2

5-L-glutamyl-4-nitroanilide + glycylglycine = 4-nitroaniline + 5-L-glutamyl-glycylglycine

736220, 735923, 736623, 736144

-

2.3.2.2

5-L-glutamyl-4-nitroanilide + glycylglycine = 4-nitroaniline + 5-L-glutamylglycylglycine

487931, 487943, 487922, 487944, 487945, 657592, 487902, 487935, 487937, 487938, 487941, 487942, 487949, 487956, 487961, 487963, 659102, 487934, 487916, 487918, 487919, 487969, 660051, 487907, 487908, 487911, 487924, 487921, 487926, 487946, 487953, 487947, 487950, 487951, 487972, 487966, 487932, 487914, 487920, 487923, 487903, 658768

-

2.3.2.2

5-L-glutamyl-4-nitroanilide + glycylglycine = 5-L-glutamyl-glycylglycine + 4-nitroaniline

720135, 707820, 719952, 718951, 717083

-

2.3.2.2

5-L-glutamyl-7-amido-4-methylcoumarin + glycylglycine = 7-amino-4-methylcoumarin + 5-L-glutamyl-glycylglycine

487931, 487915, 487917, 487929, 487936

-

2.3.2.2

5-L-glutamyl-L-leucine + glycylglycine = L-Leu + 5-L-glutamyl-glycylglycine

717083

-

2.3.2.2

9-methylanthracenylglutathione + glycylglycine = ?

735923

-

2.3.2.2

D-gamma-glutamyl-S-([4-[(4-aminophenyl)methyl]phenyl]carbamoyl)-L-cysteinylglycine + glycylglycine = S-([4-[(4-aminophenyl)methyl]phenyl]carbamoyl)-L-cysteinylglycine + L-Glu-Gly-Gly

737307

-

2.3.2.2

gamma-glutamyl-S-[(6-[[([(2R)-2-amino-3-[(carboxymethyl)amino]-3-oxopropyl]sulfanyl)carbonyl]amino]hexyl)carbamoyl]cysteinylglycine + glycylglycine = (5R,20S)-5,20-diamino-4,8,17,21-tetraoxo-7,18-dithia-3,9,16,22-tetraazatetracosane-1,24-dioic acid + L-Glu-Gly-Gly

737307

-

2.3.2.2

gamma-L-glutamyl-L-cysteinyl-glycine + glycylglycine = L-cysteinyl-glycine + 5-L-glutamyl-glycylglycine

754814

-

2.3.2.2

glutamyl-(3-carboxyl)-4-nitroanilide + glycylglycine = 3-carboxyl-4-nitroaniline + 5-L-glutamyl-glycylglycine

737262

-

2.3.2.2

glutathione disulfide + glycylglycine = L-Cys-Gly + 5-L-glutamyl-glycylglycine

754814

-

2.3.2.2

glutathione sulfonic acid + glycylglycine = ?

717083

-

2.3.2.2

glutathionesulfonic acid + glycylglycine = ?

717083

-

2.3.2.2

GSH + glycylglycine = L-Cys-Gly + 5-L-glutamyl-glycylglycine

717083

-

2.3.2.2

GSSG + glycylglycine = L-Cys-Gly + 5-L-glutamyl-glycylglycine

717083

-

2.3.2.2

hexane-1,6-diyldicarbamic acid linked GSH-GSH + glycylglycine = gamma-glutamyl-S-[(6-[[([(2R)-2-amino-3-[(carboxymethyl)amino]-3-oxopropyl]sulfanyl)carbonyl]amino]hexyl)carbamoyl]cysteinylglycine + L-Glu-Gly-Gly

737307

-

2.3.2.2

L-gamma-glutamyl-4-nitroanilide + glycylglycine = 4-nitroaniline + 5-L-glutamyl-glycyl-glycine

754814

-

2.3.2.2

L-gamma-glutamyl-4-nitroanilide + glycylglycine = 4-nitroaniline + 5-L-glutamyl-glycylglycine

756934, 757049, 752957, 757548, 758292, 754222, 756966, 756938, 757270, 757413, 757351, 756967

-

2.3.2.2

L-gamma-glutamyl-S-[(6-aminohexyl)carbamoyl]-D-cysteinylglycine + glycylglycine = [[(2R)-2-amino-3-[[(6-aminohexyl)carbamoyl]sulfanyl]propanoyl]amino]acetic acid + L-Glu-Gly-Gly

737307

-

2.3.2.2

L-glutamine + glycylglycine = NH3 + 5-L-glutamyl-glycylglycine

754814

-

2.3.2.2

L-glutamyl-gamma-7-amido-4-methylcoumarin + glycylglycine = 7-amino-4-methylcoumarin + L-glutamyl-glycylglycine

487962

-

2.3.2.2

leukotriene C4 + glycylglycine = leukotriene D4 + 5-L-glutamyl-glycylglycine

717083

-

2.3.2.2

S-(4-nitro-benzyl)glutathione + glycylglycine = ?

717083

-

2.3.2.2

S-methylglutathione + glycylglycine = ?

717083

-

2.3.2.2

56 entries

3.4.11.19

Gly-Gly + H2O = Gly + Gly

752577

-

3.4.13.12

Gly-Gly + H2O = Gly + Gly

81205

-

3.4.13.18

Gly-Gly + H2O = Gly + Gly

137176, 137193

-

3.4.13.19

Gly-Gly + H2O = Gly + Gly

647108, 35874, 647088, 647089

-

3.4.13.20

Gly-Gly + H2O = Gly + Gly

647116

-

3.4.13.5

Gly-Gly + H2O = 2 Gly

731373

-

3.4.13.5

Gly-Gly + H2O = Gly

664899

-

3.4.13.5

Gly-Gly + H2O = Gly + Gly

36081

-

3.4.13.5

3 entries

3.4.14.6

Gly-Gly + H2O = Gly-Gly-Gly-Gly

36266

-

3.4.16.4

Nalpha,Nepsilon-diacetyl-L-Lys-D-Ala-D-Ala + Gly-Gly = Nalpha,Nepsilon-diacetyl-L-Lys-D-Ala-Gly-Gly + D-Ala

36296, 36298, 28888, 36282, 36287, 36281, 36291, 36307

-

3.4.16.4

S2a + Gly-Gly = ?

670827

-

3.4.19.14

glutathione sulfonic acid + H2O + glycylglycine = ? + gamma-glutamyl-glycylglycine

717083

-

3.4.19.14

oxidized glutathione + H2O + glycylglycine = ? + gamma-glutamyl-glycylglycine

717083

-

3.4.19.14

reduced glutathione + H2O + glycylglycine = ? + gamma-glutamyl-glycylglycine

717083

-

3.4.19.14

S-(4-nitro-benzyl)glutathione + H2O + glycylglycine = ? + gamma-glutamyl-glycylglycine

717083

-

3.4.19.14

S-methylglutathione + H2O + glycylglycine = ? + gamma-glutamyl-glycylglycine

717083

-

3.4.16.4

2 entries

3.4.19.14

5 entries

3.4.22.40

Gly-Gly + H2O = ?

36712

-

3.4.24.54

Gly-Gly + H2O = ?

668856

-

3.4.24.54

Gly-Gly + H2O = Glycine + glycine

31301

-

3.4.24.54

2 entries

7.4.2.5

ATP + H2O + Gly-Gly/in = ADP + phosphate + Gly-Gly/out

735026

-

Product in Enzyme-catalyzed Reactions (69 results)

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Show Product (69 entries)

EC NUMBER

REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

2.3.2.2

5-L-glutamyglycylglycine + acceptor = glycylglycine + 5-L-glutamyl-acceptor

0

-

3.2.1.151

Glcbeta(1-4)Glcbeta(1-4)Glcbeta(1-4)Glcbeta(1-4)Glc + H2O = Glcbeta(1-4)Glcbeta(1-4)Glc + GG

0

-

3.4.11.1

Arg-Gly-Gly + H2O = Arg + Gly-Gly

651057

-

3.4.11.1

Leu-Gly-Gly + H2O = Leu + Gly-Gly

651057

-

3.4.11.10

DL-Ala-Gly-Gly + H2O = DL-Ala + Gly-Gly

81181

-

3.4.11.10

DL-Leu-Gly-Gly + H2O = DL-Leu + Gly-Gly

81181

-

3.4.11.10

L-Leu-Gly-Gly + H2O = L-Leu + Gly-Gly

0

-

3.4.11.13

Ala-Gly-Gly + H2O = Ala + Gly-Gly

81195, 81196, 81197

-

3.4.11.13

Leu-Gly-Gly + H2O = Leu + Gly-Gly

81195, 81196, 81197

-

3.4.11.13

Met-Gly-Gly + H2O = Met + Gly-Gly

81195, 81196, 81197

-

3.4.11.13

Phe-Gly-Gly + H2O = Phe + Gly-Gly

81195, 81196, 81197

-

3.4.11.13

Pro-Gly-Gly + H2O = Pro + Gly-Gly

81195, 81196, 81197

-

3.4.11.13

Ser-Gly-Gly + H2O = Ser + Gly-Gly

81195, 81196, 81197

-

3.4.11.13

Val-Gly-Gly + H2O = Val + Gly-Gly

81195, 81196, 81197

-

3.4.11.15

Lys-Gly-Gly + H2O = Lys + Gly-Gly

0

-

3.4.11.15

Met-Gly-Gly + H2O = Met + Gly-Gly

647039

-

3.4.11.17

Leu-Gly-Gly + H2O = Leu + Gly-Gly

81203

-

3.4.11.17

Val-Gly-Gly + H2O = Val + Gly-Gly

81203

-

3.4.11.1

2 entries

3.4.11.10

3 entries

3.4.11.13

7 entries

3.4.11.15

2 entries

3.4.11.17

2 entries

3.4.11.18

Met-Gly-Gly + H2O = Met + Gly-Gly

0

-

3.4.11.19

D-Ala-Gly-Gly + H2O = D-Ala + Gly-Gly

0

-

3.4.11.23

Xaa-Gly-Gly + H2O = Xaa + Gly-Gly

643878

-

3.4.11.24

Leu-Gly-Gly + H2O = Leu + Gly-Gly

651836

-

3.4.11.4

Gly-Gly-Gly + H2O = Gly + Gly-Gly

0

-

3.4.11.4

L-Ala-Gly-Gly + H2O = L-Ala + Gly-Gly

0

-

3.4.11.4

L-Phe-Gly-Gly + H2O = L-Phe + Gly-Gly

35921, 0

-

3.4.11.4

L-Pro-Gly-Gly + H2O = L-Pro + Gly-Gly

0

-

3.4.11.4

Leu-Gly-Gly + H2O = Leu + Gly-Gly

0, 35928, 35931, 35925, 649359

-

3.4.11.4

Lys-Gly-Gly + H2O = Lys + Gly-Gly

649359

-

3.4.11.4

Met-Gly-Gly + H2O = Met + Gly-Gly

0, 649359

-

3.4.11.4

Tyr-Gly-Gly + H2O = Tyr + Gly-Gly

649359

-

3.4.11.4

8 entries

3.4.11.5

Pro-Gly-Gly + H2O = Pro + Gly-Gly

0

-

3.4.13.17

D-Leu-Gly-Gly + H2O = D-Leu + Gly-Gly

81206

-

3.4.13.17

Gly-Gly-D-Leu + H2O = Gly-Gly + D-Leu

81206

-

3.4.13.19

L-cystinyl-bis-Gly + H2O = L-Cys + Gly-Gly

0

-

3.4.13.19

L-cystinyl-bis-glycine + H2O = L-Cys + Gly-Gly

0

-

3.4.14.1

Gly-Gly-ethyl ester + H2O = Gly-Gly + ethanol

36131

-

3.4.14.1

Gly-Gly-Gly + H2O = Gly-Gly + Gly

36146

-

3.4.14.1

Gly-Gly-Phe-NH2 + H2O = Gly-Gly + Phe-NH2

0

-

3.4.14.1

tetraglycine + H2O = Gly-Gly

36146

-

3.4.13.17

2 entries

3.4.13.19

2 entries

3.4.14.1

4 entries

3.4.14.11

Gly-Pro-Gly-Gly + H2O = Gly-Pro + Gly-Gly

0

-

3.4.14.2

Gly-Pro-Gly-Gly + H2O = Gly-Pro + Gly-Gly

0

-

3.4.14.6

Gly-Gly-Gly-Gly + H2O = Gly-Gly

36266

-

3.4.15.1

1-dimethylaminonaphthalene-5-sulfonyl-Gly-Gly-Gly + H2O = 1-dimethylaminonaphthalene-5-sulfonyl-Gly + Gly-Gly

0

-

3.4.15.1

2-furanacryloyl-Phe-Gly-Gly + H2O = 2-furanacryloyl-Phe + Gly-Gly

0

-

3.4.15.1

3-hydroxybutyryl-Gly-Gly-Gly + H2O = 3-hydroxybutyryl-Gly + Gly-Gly

0

-

3.4.15.1

3-hydroxybutyrylglycyl-glycyl-glycine + H2O = 3-hydroxybutyrylglycine + Gly-Gly

0

-

3.4.15.1

benzoyl-Gly-Gly-Gly + H2O = benzoyl-Gly + Gly-Gly

0

-

3.4.15.1

benzyloxycarbonyl-Gly-Gly-Gly + H2O = benzyloxycarbonyl-Gly + Gly-Gly

0

-

3.4.15.1

benzyloxycarbonyl-Leu-Gly-Gly + H2O = benzyloxycarbonyl-Leu + Gly-Gly

0

-

3.4.15.1

furanacryloyl-L-Phe-Gly-Gly + H2O = furanacryloyl-L-Phe + Gly-Gly

0

-

3.4.15.1

Gly-Gly-Tyr-Arg + H2O = Gly-Gly + Tyr-Arg

81238

-

3.4.15.1

hippuryl-Gly-Gly + H2O = hippuric acid + Gly-Gly

0

-

3.4.15.1

N-[3-(2-furyl)acryloyl]-Phe-Gly-Gly + H2O = N-[3-(2-furyl)acryloyl]-Phe + Gly-Gly

0

-

3.4.15.1

Tyr-Gly-Gly + H2O = Tyr + Gly-Gly

0

-

3.4.15.1

N-[3-(2-furyl)acryloyl]-L-phenylalanyl-glycyl-glycine + H2O = N-[3-(2-furyl)acryloyl]-L-phenylalanine + glycyl-glycine

0

-

3.4.15.1

13 entries

3.4.15.5

Gly-Gly-Phe-Ala + H2O = Gly-Gly + Phe-Ala

28733

-

3.4.17.12

Gly-Gly-Arg + H2O = Gly-Gly + Arg

0

-

3.4.19.5

beta-Asp-Gly-Gly + H2O = Asp + Gly-Gly

647271

-

3.4.22.B60

Z-Gly-Pro-Gly-Gly-Pro-Ala + H2O = Z-Gly-Pro + Gly-Gly + L-Pro-L-Ala

0

-

3.4.24.75

pentaglycine + H2O = diglycine + triglycine

0

-

3.4.24.77

Gly-Gly-Phe-Leu + H2O = Gly-Gly + Phe-Leu

0

-

3.4.24.B14

Gly-Gly-Phe-Met + H2O = Gly-Gly + Phe-Met

0

-

3.5.1.32

glycylglycylglycine + H2O = glycine + glycylglycine

172035

-

3.5.1.58

N-benzyl-Gly-Gly + H2O = benzyl alcohol + Gly-Gly

0

-

3.5.1.58

N-benzyloxycarbonyl-Gly-Gly + H2O = benzyl alcohol + CO2 + Gly-Gly

209204, 0

-

3.5.1.58

2 entries

3.5.2.13

2,5-dioxopiperazine + H2O = glycylglycine

172085

-

6.3.2.4

ATP + Gly = ADP + phosphate + Gly-Gly

0

-

6.3.2.4

glycine + glycine + ATP = ADP + Gly-Gly + phosphate

0

-

6.3.2.4

2 entries

7.4.2.5

ATP + H2O + Gly-Gly/in = ADP + phosphate + Gly-Gly/out

0

-

Activator in Enzyme-catalyzed Reactions (9 results)

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Show Activating Compound (9 entries)

EC NUMBER

COMMENTARY

LITERATURE

ENZYME 3D STRUCTURE

1.1.1.44

-

286825

-

2.3.2.2

enhances activity

660557

-

3.1.3.2

activates enzyme form A and B

134717

-

3.1.4.35

-

135338

-

3.4.22.37

activates only RGP-B

638849

-

3.4.22.37

increases the substrate hydrolysis, increases Km and kcat value

650464

-

3.4.22.37

stimulates the amidolytic activity and limited proteolysis, but destabilizes the enzyme

651891

-

3.4.22.37

stimulates the amidolytic activity and limited proteolysis, but destabilizes the isozymes

651891

-

3.4.22.37

stimulates depending on the substrate

668785

-

3.4.22.37

5 entries

Inhibitor in Enzyme-catalyzed Reactions (20 results)

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Show Inhibitors (20 entries)

EC NUMBER

COMMENTARY

LITERATURE

ENZYME 3D STRUCTURE

2.2.1.10

slightly inhibiting as buffer at 50 mM

692386

-

2.3.2.2

-

487932

-

2.3.2.2

high concentration, pH 6.0-7.5

487921

-

2.3.2.2

high concentration, with L-Glu-4-nitroanilide, not glutathione as donor

487907

-

2.3.2.2

3 entries

2.4.1.34

0.75 M

489053

-

3.1.3.1

-

693394

-

3.2.1.33

inhibits at acidic pH

171378

-

3.2.1.33

no inhibition at 0.01 or 0.05 M

171379

-

3.2.1.33

slight inhibition

171377

-

3.2.1.33

3 entries

3.4.11.6

5 mM, 8% inhibition

651488

-

3.4.22.47

200 mM, 50% inhibition

638843

-

3.5.1.1

-

208940

-

3.5.1.3

competitive inhibitor, Ki: 5 mM

288884

-

4.1.1.38

higher inhibition at pH 7.8 than at pH 6.5

33091

-

4.1.2.12

-

4901

-

4.2.1.49

highly specific

5771

-

4.2.1.49

reactivatable thermally

5770

-

4.2.1.49

2 entries

4.3.1.17

-

210794

-

6.3.2.4

-

1235

-

6.3.2.4

-

745681

-

6.3.2.4

2 entries

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

1.97.1.12

6zzy, 3D-view

1.97.1.12

7a4p, 3D-view

1.97.1.12

6zzy, 3D-view

1.97.1.12

7a4p, 3D-view

1.97.1.12

6zzy, 3D-view

1.97.1.12

7a4p, 3D-view

1.97.1.12

6zzy, 3D-view

1.97.1.12

7a4p, 3D-view

1.97.1.12

6zzy, 3D-view

1.97.1.12

7a4p, 3D-view

1.97.1.12

6zzy, 3D-view

1.97.1.12

7a4p, 3D-view

1.97.1.12

6zzy, 3D-view

1.97.1.12

7a4p, 3D-view

1.97.1.12

6zzy, 3D-view

1.97.1.12

7a4p, 3D-view

1.97.1.12

16 entries

Enzyme Kinetic Parameters

k_cat Value (Turnover Number) (2 results)

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Show Turnover Number (2 entries)

EC NUMBER

TURNOVER NUMBER [1/S]

TURNOVER NUMBER MAXIMUM [1/S]

COMMENTARY

LITERATURE

3.4.11.1

10860

-

His-tagged recombinant enzyme, 37°C

651057

3.4.11.1

10900

-

His-tagged recombinant enzyme, 37°C

651057

3.4.11.1

2 entries

K_M Value (25 results)

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Show KM Value (25 entries)

EC NUMBER

KM VALUE [MM]

KM VALUE MAXIMUM [MM]

COMMENTARY

LITERATURE

2.3.2.2

0.007

-

pH 7.4, 37°C

757548

2.3.2.2

0.687

-

pH 8.0, 37°C

701909

2.3.2.2

0.7

-

recombinant mutant R109E, pH 9.0, 60°C

754222

2.3.2.2

0.8

-

recombinant mutant R109F, pH 9.0, 60°C

754222

2.3.2.2

0.94

-

recombinant wild-type enzyme, pH 9.0, 60°C

754222

2.3.2.2

1.28

-

-

487962

2.3.2.2

1.5

-

recombinant mutant R109K, pH 9.0, 60°C

754222

2.3.2.2

1.6

-

recombinant mutant R109S, pH 9.0, 60°C

754222

2.3.2.2

2.5

-

37°C, pH 8.0

674593

2.3.2.2

2.9

2.96

-

487946

2.3.2.2

2.9

2.96

rat kidney enzyme

487930

2.3.2.2

2.9

2.96

recombinant wild-type enzyme

487961

2.3.2.2

3.4

-

recombinant mutant enzyme

487961

2.3.2.2

4

-

with 0.8 mM L-Glu-4-nitroanilide, kidney enzyme

487899

2.3.2.2

4

4.7

L-Met, rat kidney enzyme

487930

2.3.2.2

4.35

-

with 1.6 mM L-Glu-4-nitroanilide, kidney enzyme

487899

2.3.2.2

7.6

-

-

487920

2.3.2.2

10

-

-

487908

2.3.2.2

12.4

-

-

487941

2.3.2.2

16.9

-

-

659102

2.3.2.2

20

-

-

487919

2.3.2.2

48

-

-

487950

2.3.2.2

590

-

-

487944

2.3.2.2

23 entries

3.4.11.1

11.2

-

His-tagged recombinant enzyme, 37°C

651057

3.4.22.40

10.1

-

-

36712

References & Links

Literature References (176)

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Show Reference (176 entries)

BRENDA REFERENCE ID

PUBMED ID

TITLE

YEAR

AUTHORS

JOURNAL

VOLUME

PAGES

1235

4552992

Studies on Escherichia coli enzymes involved in the synthesis of uridine diphosphate-N-acetyl-muramyl-pentapeptide

1972

Lugtenberg, E.J.J.

J. Bacteriol.

110

26-34

4901

13475336

Ketopantoate formation by a hydroxymethylation enzyme from Escherichia coli

1957

McIntosh, E.N.; Purko, M.; Wood, W.A.

J. Biol. Chem.

228

499-510

5770

2570140

Thermal activation of photoactivatable urocanase from Pseudomonas putida

1989

O'Donnell, P.S.; Hug, D.H.

J. Photochem. Photobiol. B, Biol.

3

429-435

5771

2577699

Specific inhibition of bacterial and bovine urocanase by glycylglycine

1989

Hunter, J.K.; Hug, D.H.

Pept. Res.

2

240-245

28733

13271

Dipeptidyl carboxypeptidase from Escherichia coli

1976

Yaron, A.

Methods Enzymol.

45

599-610

28888

4464852

Molecular weight, amino acid composition and physicochemical properties of the exocellular DD-carboxypeptidase-transpeptidase of Streptomyces R39

1974

Frere, J.M.; Moreno, R.; Ghuysen, J.M.; Perkins, H.R.; Dierickx, L.; Delcambe, L.

Biochem. J.

143

233-240

31301

3904081

Characterization of mucrotoxin A from the venom of Trimeresurus mucrosquamatus (the Chinese habu snake)

1985

Kishida, M.; Nikai, T.; Mori, N.; Kohmura, S.; Sugihara, H.

Toxicon

23

637-645

33091

4288896

Phosphoenolpyruvate carboxytransphosphorylase. II. Crystallization and properties

1966

Lochmueller, H.; Wood, H.G.; Davis, J.J.

J. Biol. Chem.

241

5678-5691

35874

6122685

Glutathione-degrading enzymes of microvillus membranes

1982

Kozak, E.M.; Tate, S.S.

J. Biol. Chem.

257

6322-6327

35921

3881261

Purification and characterization of two aminopeptidases from guinea-pig small-intestinal mucosa. Cavian intestinal tripeptide hydrolases

1985

Morgan, J.G.; Donlan, J.

Eur. J. Biochem.

146

429-435

35925

6771256

Isolation and characterization of aminotripeptidase from monkey brain

1980

Hayashi, M.; Oshima, K.

J. Biochem.

87

1403-1411

35928

356879

Tripeptide-specific aminopeptidase from Escherichia coli AJ005

1978

Hermsdorf, C.L.

Biochemistry

17

3370-3376

35931

4694732

Aminotripeptidase of swine kidney. I. Isolation and characterization of three different forms; utility of the enzyme in sequence work

1973

Chenoweth, D.; Mitchel, R.E.J.; Smith, E.L.

J. Biol. Chem.

248

1672-1683

36081

-

Properties of Nalpha-acetylhistidine deacetylase in brain of rainbow trout Oncorhynchus mykiss

1993

Yamada, S.; Tanaka, Y.; Sameshima, M.; Furuichi, M.

Comp. Biochem. Physiol. B

106

309-315

36131

5758556

The specificity of dipeptidyl transferase

1968

Voynick, I.M.; Fruton, J.S.

Biochemistry

7

40-44

36146

4306035

New observations on the substrate specificity of cathepsin C (dipeptidyl aminopeptidase I). Including the degradation of beta-corticotropin and other peptide hormones

1969

McDonald, J.K.; Zeitman, B.B.; Reilly, T.J.; Ellis, S.

J. Biol. Chem.

244

2693-2709

36266

-

Dipeptidyl tetrapeptide hyrolase, a new enzyme with dipeptidyl ligase activity

1984

Eng, F.W.H.T.

Can. J. Biochem. Cell Biol.

62

516-528

36281

3888533

Penicillin-sensitive enzymes in peptidoglycan biosynthesis

1985

Frere, J.M.; Joris, B.

CRC Crit. Rev. Microbiol.

11

299-396

36282

6597561

Bacterial wall peptidoglycan, DD-peptidases and beta-lactam antibiotics

1984

Ghuysen, J.M.; Frere, J.M.; Leyh-Bouille, M.; Nguyen-Disteche, M.; Coyette, J.; Dusart, J.; Charlier, P.; Dive, G.; Lamotte-Brasseur, J.

Scand. J. Infect. Dis.

42

17-37

36287

7238522

On the DD-carboxypeptidase enzyme system of Streptomyces strain K15

1981

Leyh-Bouille, M.; Nguyen-Disteche, M.; Ghuysen, J.M.

Eur. J. Biochem.

115

579-584

36291

3997832

2.8-A Structure of penicillin-sensitive D-alanyl carboxypeptidase-transpeptidase from Streptomyces R61 and complexes with beta-lactams

1985

Kelly, J.A.; Knox, J.R.; Moews, P.C.; Hite, G.J.; Bartolone, J.B.; Zhao, H.; Joris, B.; Frere, J.M.; Ghuysen, J.M.

J. Biol. Chem.

260

6449-6458

36296

10161

Membrane-bound DD-carboxypeptidase and transpeptidase activities from Bacillus megaterium KM at pH 7. General properties, substrate specificity and inhibition by beta-lactam antibiotics

1976

Marquet, A.; Nieto, M.; Diaz-Maurino, T.

Eur. J. Biochem.

68

581-589

36298

4209348

Membrane-bound DD-carboxypeptidase and LD-transpeptidase of Streptococcus faecalis ATCC 9790

1974

Coyette, J.; Perkins, H.R.; Polacheck, I.; Shockman, G.D; Ghuysen, J.M.

Eur. J. Biochem.

44

459-468

36307

1445284

Secretion by overexpression and purification of the water-soluble Streptomyces K15 DD-transpeptidase/penicillin-binding protein

1992

Palomeque-Messia, P.; Quittre, V.; Leyh-Bouille, M.; Nguyen-Disteche, M.; Gershater, C.J.L.; Dacey, I.K.; Dusart, J.; van Beeumen, J.; Ghuysen, J.M.

Biochem. J.

288

87-91

36712

9546047

Catalytic properties of the cysteine aminopeptidase PepC, a bacterial bleomycin hydrolase

1998

Mistou, M.Y.; Gripon, J.C.

Biochim. Biophys. Acta

1383

63-70

81181

4961737

Aeromonas aminopeptidase: purification and some general properties

1966

Prescott, J.M.; Wilkes, S.H.

Arch. Biochem. Biophys.

117

328-336

81195

4318

An extracellular aminopeptidase from Clostridium histolyticum

1976

Kessler, E.; Yaron, A.

Eur. J. Biochem.

63

271-287

81196

13266

Extracellular aminopeptidase from Clostridium histolyticum

1976

Kessler, E.; Yaron, A.

Methods Enzymol.

45

544-552

81197

4631895

A novel aminopeptidase from Clostridium histolyticum

1973

Kessler, E.; Yaron, A.

Biochem. Biophys. Res. Commun.

50

405-412

81203

-

Crystallization and characterization of a novel aminopeptidase from Trichosporon cutaneum

1983

Iwayama, A.; Kimura, T.; Adachi, O.; Ameyama, M.

Agric. Biol. Chem.

47

2483-2493

81205

4567782

Purification and properties of dipeptidase M from Escherichia coli B

1973

Brown, J.L.

J. Biol. Chem.

248

409-416

81206

6444201

Peptidyl-D-amino acid hydrolase from Loligo vulgaris Lam. Purification and characterization

1984

D'Aniello, A.; Strazullo, L.

J. Biol. Chem.

259

4237-4243

81238

2999099

Angiotensin-converting enzyme from human tissues. Physicochemical, catalytic, and immunological properties

1985

Lanzillo, J.J.; Stevens, J.; Dasarathy, Y.; Yotsumoto, H.; Fanburg, B.L.

J. Biol. Chem.

260

14938-14944

134717

4004260

Resolution of the low-molecular-weight acid phosphatase in avian pectoral muscle into two distinct enzyme forms

1985

Baxter, J.H.; Suelter, C.H.

Arch. Biochem. Biophys.

239

29-37

135338

4365412

Guanosine 3',5'-cyclic monophosphate phosphodiesterase activity of Bacillus licheniformis

1974

Hwang, T.C.; Clark, V.L.; Bernlohr, R.W.

Biochem. Biophys. Res. Commun.

58

707-713

137176

2378680

Separation and characterization of two carnosine-splitting cytosolic dipeptidases from hog kidney (carnosinase and non-specific dipeptidase)

1990

Lenney, J.F.

Biol. Chem. Hoppe-Seyler

371

433-440

137193

2303

Purification and specificity of prolyl dipeptidase from bovine kidney

1976

Akrawi, A.F.; Bailey, G.S.

Biochim. Biophys. Acta

422

170-178

171377

-

Enzymes of glycogen debranching: amylo-1,6-glucosidase (I) and oligo-1,4 -> 1,4-glucantransferase (II)

1966

Brown, D.H.; Illingworth Brown, B.

Methods Enzymol.

8

515-524

171378

-

Rabbit muscle amylo-1,6-glucosidase: properties and evidence of heterogeneity

1968

Taylor, P.M.; Whelan, W.J.

Control of Glycogen Metabolism, Proc. FEBS 4th Meeting, Oslo, 1967 (Whelan, W. J. , ed. )

-

101-114

171379

5805288

Purification and properties of rabbit muscle amylo-1,6-glucosidase-oligo-1,4->1,4-transferase

1969

Nelson, T.E.; Kolb, E.; Larner, J.

Biochemistry

8

1419-1428

172035

-

Hippurathydrolase, ein neues Enzym aus Mikroorganismen, Darstellung einer gereinigten Enzympräparation und Untersuchungen zur Substratspezifität

1968

Röhr, M.

Monatsh. Chem.

99

2255-2277

172085

-

Purification and some properties of cyclo(Gly-Gly) hydrolase from a strain of Bacillus sp. No. 106

1985

Muro, T.; Tominaga, Y.; Okada, S.

Agric. Biol. Chem.

49

1567-1572

208940

7259189

Purification and properties of asparaginase from Lupinus arboreus and Lupinus angustifolius

1981

Chang, K.S.; Farnden, K.J.F.

Arch. Biochem. Biophys.

208

49-58

209204

-

A new enzyme Nalpha-benzyloxy-carbonyl moiety hydrolytic enzyme, from Streptococcus faecalis R

1984

Murao, S.; Matsumura, E.; Shin, T.; Kawano, T.

Agric. Biol. Chem.

48

1673-1675

210794

2065681

Purification and properties of an iron-sulfur containing and pyridoxal-phosphate-independent L-serine dehydratase from Peptostreptococcus asaccharolyticus

1991

Grabowski, R.; Buckel, W.

Eur. J. Biochem.

199

89-94

286825

4672667

6-phosphogluconate dehydrogenase and the assay of uridine diphosphate glucose pyrophosphorylase in the cellular slime mould Dictyostelium discoideum

1972

Emundson, T.D.; Ashworth, J.M.

Biochem. J.

126

593-600

288884

3003502

alpha-Keto acid omega-amidase from rat liver

1985

Cooper, A.J.L.; Duffy, T.E.; Meister, A.

Methods Enzymol.

113

350-358

485964

-

Amidinotranferases

1973

Walker, J.B.

The Enzymes, 3rd Ed. (Boyer, P. D. , ed. )

9

497-509

485981

5935341

Enzymic studies on the biosynthesis of streptomycin

1966

Walker, M.S.; Walker, J.B.

J. Biol. Chem.

241

1262-1270

485984

1134367

L-Arginine:inosamine-P amindinotransferase (s)

1975

Walker, J.B.

Methods Enzymol.

43

451-458

485989

9922132

Crystal Structure of L-Arginine:Inosamine-Phosphate Amidinotransferase StrB1 from Streptomyces griseus: An Enzyme Involved in Streptomycin Biosynthesis

1998

Fritsche, E.; Bergner, A.; Humm, A.; Piepersberg, W.; Huber, R.

Biochemistry

37

17664-17672

487897

1978610

Purification and properties of gamma-glutamyl transpeptidase from human testis

1990

Yoshida, K.I.; Arai, K.; Kobayashi, N.; Saitoh, H.

Andrologia

22

239-246

487899

-

Partial purification and characterization of gamma-glutamyl transpeptidase from rat kidney

1986

Kimm, S.W.; Kim, E.G.; Park, S.C.

Korean J. Biochem.

18

135-143

487902

6150450

Solubilization and some properties of gamma-glutamyltransferase from human brain microvessels

1984

Vesely, J.; Cernoch, M.

Neurochem. Res.

9

927-934

487903

-

Studies on the properties of the variants of gamma-glutamyl transpeptidase in human urine

1982

Rambabu, K.; Pattabiraman, T.N.

J. Biosci.

4

287-294

487907

-

Some properties of gamma-glutamyltransferase from hog small intestine

1981

Nakamura, Y.; Kato, H.; Suzuki, F.; Nagata, Y.

Biomed. Res.

2

509-516

487908

6114882

Purification and properties of gamma-glutamyl transpeptidase from bovine parotid gland

1981

Hata, K.; Hayakawa, M.; Abiko, Y.; Takiguchi, H.

Int. J. Biochem.

13

681-692

487911

42549

gamma-Glutamyl transpeptidase of bovine ciliary body: purification and properties

1979

Das, N.D.; Shichi, H.

Exp. Eye Res.

29

109-121

487914

39603

Purification and comparison of several catalytic parameters of the gamma-glutamyltranspeptidase of rat mammary adenocarcinoma (13762) and of normal rat mammary gland

1979

Jaken, S.; Mason, M.

Biochim. Biophys. Acta

568

331-338

487915

6102936

The purification of gamma-glutamyltransferase from normal rat liver

1980

Ding, J.L.; Smith, G.D.; Peters, T.J.

Biochem. Soc. Trans.

8

77

487916

6102912

Latent active site in rat-kidney gamma-glutamyl transpeptidase. The refolding process of the large subunit and characterization of the renatured enzyme

1980

Horiuchi, S.; Inoue, M.; Morino, Y.

Eur. J. Biochem.

105

93-102

487917

6111348

Purification and properties of gamma-glutamyl transferase from normal rat liver

1981

Ding, J.L.; Smith, G.D.; Peters, T.J.

Biochim. Biophys. Acta

657

334-343

487918

6139125

Phenobarbital and related compounds as novel inhibitors of gamma-glutamyltranspeptidase

1983

Sachdev, G.P.; Leahy, D.S.; Chace, K.V.

Biochim. Biophys. Acta

749

125-129

487919

6128031

Purification and characterization of gamma-glutamyltransferase from rat pancreas

1982

Takahashi, S.; Steinman, H.M.; Ball, D.

Biochim. Biophys. Acta

707

66-73

487920

6152628

Purification and properties of gamma-glutamyl transpeptidase from rat deciduoma

1984

Tarachand, U.

J. Appl. Biochem.

6

278-288

487921

6113845

Some kinetic properties of gamma-glutamyltransferase from rabbit liver

1981

Bagrel, D.; Petitclerc, C.; Schiele, F.; Siest, G.

Biochim. Biophys. Acta

658

220-231

487922

36916

Identification, partial purification and biochemical characterization of gamma-glutamyltranspeptidase present as a membrane component in skimmed milk and milk fat-globule membranes, and in mammary-tumour virus from the milk of infected mice

1979

Franþois, C.; Calberg-Bacq, C.M.; Gosselin, L.; Kozma, S.; Osterrieth, P.M.

Biochim. Biophys. Acta

567

106-115

487923

32176

Purification and enzymatic properties of gamma-glutamyltransferase from bovine colostrum

1978

Yasumoto, K.; Iwami, K.; Fushiki, T.; Mitsuda, H.

J. Biochem.

84

1227-1236

487924

6135696

Purification and properties of bovine liver gamma-glutamyltransferase

1983

Furukawa, M.; Higashi, T.; Tateishi, N.; Ochi, K.; Sakamoto, Y.

J. Biochem.

93

839-846

487926

1275

gamma-Glutamyl transpeptidase of sheep-kidney cortex. Isolation, catalytic properties and dissociation into two polypeptide chains

1976

Zelazo, P.; Orlowski, M.

Eur. J. Biochem.

61

147-155

487929

6127596

gamma-Glutamyl transpeptidase, a leukotriene metabolizing enzyme

1982

Bernström, K.; Orning, L.; Hammarström, S.

Methods Enzymol.

86

38-45

487930

2868391

gamma-Glutamyl transpeptidase: kinetics and mechanism

1985

Allison, D.

Methods Enzymol.

113

419-437

487931

2868390

gamma-Glutamyl transpeptidase from kidney

1985

Tate, S.S.; Meister, A.

Methods Enzymol.

113

400-419

487932

-

gamma-Glutamyltransferase. (gamma-Glutamyl)-peptide:amino acid gamma-glutamyltransferase, EC 2.3.2.2. 1. General

1983

Shaw, L.M.

Methods Enzym. Anal. , 3rd Ed. (Bergmeyer, H. U. , ed. )

3

349-352

487933

-

gamma-Glutamyltransferase. (gamma-Glutamyl)-peptide:amino acid gamma-glutamyltransferase, EC 2.3.2.2. 2. Routine method

1983

Wahlefeld, A.W.; Bergmeyer, H.U.

Methods Enzym. Anal. , 3rd Ed. (Bergmeyer, H. U. , ed. )

3

352-356

487934

-

gamma-Glutamyltransferase. (gamma-Glutamyl)-peptide:amino acid gamma-glutamyltransferase, EC 2.3.2.2. 3. IFCC reference method (provisional)

1983

Shaw, L.M.; Stromme, J.H.

Methods Enzym. Anal. , 3rd Ed. (Bergmeyer, H. U. , ed. )

3

357-364

487935

6112969

gamma-Glutamyl transpeptidase from WI-38 fibroblasts: purification and active site modification studies

1981

Takahashi, S.; Zukin, R.S.; Steinman, H.M.

Arch. Biochem. Biophys.

207

87-95

487936

2859051

Purification of gamma-glutamyltransferase by phenyl boronate affinity chromatography. Studies on the acceptor specificity of transpeptidation by rat kidney gamma-glutamyltransferase

1985

Cook, N.D.; Peters, T.J.

Biochim. Biophys. Acta

828

205-212

487937

4442

Studies of human kidney gamma-glutamyl transpeptidase. Purification and structural, kinetic and immunological properties

1976

Miller, S.P.; Awasthi, Y.C.; Srivastava, S.K.

J. Biol. Chem.

251

2271-2278

487938

19463

Human kidney gamma-glutamyl transpeptidase. Catalytic properties, subunit structure, and localization of the gamma-glutamyl binding site on the light subunit

1977

Tate, S.S.; Ross, M.E.

J. Biol. Chem.

252

6042-6045

487941

18197

Purification and some properties of gamma-glutamyltransferase from human liver

1977

Huseby, N.

Biochim. Biophys. Acta

483

46-56

487942

18198

Partial purification and some properties of gamma-glutamyl transpeptidase from human bile

1977

Indirani, N.; Hill, P.G.

Biochim. Biophys. Acta

483

57-62

487943

1371053

Purification and properties of gamma-glutamyltranspeptidase from Bacillus subtilis (natto)

1991

Ogawa, Y.; Hosoyama, H.; Hamano, M.; Motai, H.

Agric. Biol. Chem.

55

2971-2977

487944

2877974

gamma-Glutamyltranspeptidase from Escherichia coli K-12: purification and properties

1986

Suzuki, H.; Kumagai, H.; Tochikura, T.

J. Bacteriol.

168

1325-1331

487945

2877975

gamma-Glutamyltranspeptidase from Escherichia coli K-12: formation and localization

1986

Suzuki, H.; Kumagai, H.; Tochikura, T.

J. Bacteriol.

168

1332-1335

487946

6148333

Purification and properties of gamma-glutamyltranspeptidase from Proteus mirabilis

1984

Nakayama, R.; Kumagai, H.; Tochikura, T.

J. Bacteriol.

160

341-346

487947

-

Properties of gamma-glutamyltransferase from Lentinus edodes

1975

Iwami, K.; Yasumoto, K.; Nakamura, K.; Mitsuda, H.

Agric. Biol. Chem.

39

1933-1940

487949

35101

Isolation of anthglutin, an inhibitor of gamma-glutamyl transpeptidase from Penicillum oxalicum

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