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Ligand peptide

Basic Ligand Information

Molecular Structure

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Roles as Enzyme Ligand

In Vivo Substrate in Enzyme-catalyzed Reactions (18 results)

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Show Natural Substrate (18 entries)

EC NUMBER

PROVEN IN VIVO REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

2.3.1.255

acetyl-CoA + peptide = CoA + Nalpha-acetylpeptide

720453, 657745

-

2.3.1.255

acetyl-CoA + peptide = Nalpha-acetylpeptide + CoA

702871, 705613, 706924

-

2.3.1.255

2 entries

2.3.1.257

acetyl-CoA + peptide = CoA + Nalpha-acetylpeptide

720835

-

2.3.1.258

acetyl-CoA + peptide = CoA + Nalpha-acetylpeptide

719976, 720002

-

2.3.1.5

acetyl-CoA + peptide = CoA + Nalpha-acetylpeptide

487664

-

3.4.11.10

Peptides + H2O = ?

81179, 81170, 81178, 81177, 81176, 81175, 81173, 81172, 81171, 81174, 81180, 81181, 81182, 81183, 81184, 81185, 81186, 81187, 81189, 81190, 81188

-

3.4.11.13

Peptides + H2O = ?

81193, 81194, 81195, 81196, 81197

-

3.4.11.16

Peptides + H2O = ?

643874, 643871, 643872, 643877, 643870

-

3.4.11.24

peptide + H2O = ?

649123, 651036, 651038, 651033, 653836, 653768, 652775, 652773, 651836, 651046

-

3.4.11.3

Peptides + H2O = ?

35919, 35907

-

3.4.17.B1

peptide + H2O = ?

651211, 651034, 649646

-

3.4.21.26

Peptides + H2O = ?

81340, 81344

-

3.4.22.48

peptide + H2O = peptide proteolytically cleaved into fragments or single amino acids

643963, 643962, 643966

-

3.4.22.B28

peptide + H2O = hydrolyzed peptide

648094

-

3.4.22.B30

peptide + H2O = hydrolyzed peptide

648105, 395498

-

3.4.22.B31

peptide + H2O = hydrolyzed peptide

395498

-

3.4.22.B36

peptide + H2O = hydrolyzed peptide

648415

-

3.4.23.12

Peptides + H2O = ?

36777, 36778, 36773, 36774, 36771, 36772, 36775, 36776

-

In Vivo Product in Enzyme-catalyzed Reactions (69 results)

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Show Natural Product (69 entries)

EC NUMBER

PROVEN IN VIVO REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

2.3.2.2

a (5-L-glutamyl)-peptide + an amino acid = a peptide + a 5-L-glutamyl amino acid

-

-

2.3.2.2

(5-L-glutamyl)-peptide + acceptor + H+ = peptide + 5-L-glutamyl amino acid

, 487962, 487968, 487930, 487967

-

2.3.2.2

(5-L-glutamyl)-peptide + an amino acid = peptide + 5-L-Glu-Xaa

-

-

2.3.2.2

(5-L-glutamyl)-peptide + an amino acid = peptide + a 5-L-glutamyl amino acid

-

-

3.1.1.29

peptidyl-tRNA + H2O = peptide + tRNA

-

-

3.1.1.29

peptidyl-tRNAL + H2O = peptide + tRNA

-

-

3.1.1.29

peptidyl-tRNALys + H2O = peptide + tRNALys

-

-

2.3.2.2

4 entries

3.1.1.29

3 entries

3.4.11.18

Met-peptide + H2O = Met + peptide

-

-

3.4.11.23

Xaa-peptide + H2O = Xaa + peptide

643878

-

3.4.17.B1

protein + H2O = peptides

649646, 651211, 651034

-

3.4.19.3

pyroglutamyl-peptide + H2O = pyroglutamate + peptide

652124

-

3.4.21.10

proacrosin + H2O = acrosin + peptide

-

-

3.4.21.102

pre-D1 protein + H2O = D1 protein + peptide

-

-

3.4.21.117

polypeptide + H2O = peptides

647346, 647348, 647331, 647344, 647349, 647347, 647342, 647343, 647345, 647332

-

3.4.21.118

polypeptide + H2O = peptides

647331, 647322, 647325, 647326, 647328, 647329, 647324, 647332, 647323, 647327, 647321

-

3.4.21.119

polypeptide + H2O = peptides

647369, 647370, 647371, 647372, 647373

-

3.4.21.20

factor VIII + H2O = factor VIIIa + peptide

-

-

3.4.21.20

factor VIIIa + H2O = factor VIII + peptide

-

-

3.4.21.20

RANTES 1-68 + H2O = RANTES 4-68 + peptide

-

-

3.4.21.20

3 entries

3.4.21.35

polypeptide + H2O = peptides

647332, 647361, 647483, 647485, 647486, 647487, 647488, 647497, 647498, 647500, 647501, 647502, 647503, 647506, 647508, 647509, 647510, 647512, 647513, 647514, 647519, 647522, 647523, 647531, 647536, 647537, 647540, 647542, 647331, 647480, 647482, 647494, 647495, 647496, 647504, 647505, 647530, 95367, 647481, 647484, 647491, 647492, 647499, 647517, 647511, 395498, 647515, 647489

-

3.4.21.77

polypeptide + H2O = peptides

647587, 647588, 647590, 647591, 647592, 647594, 647589, 647332

-

3.4.21.89

intermediate of cytochrome c peroxidase + H2O = mature cytochrome c peroxidase + peptide

-

-

3.4.21.B10

polypeptide + H2O = peptides

647332

-

3.4.21.B12

polypeptide + H2O = peptides

647333, 647339, 647332, 647334, 647335, 647337, 647336, 647338

-

3.4.21.B3

polypeptide + H2O = peptides

-

-

3.4.21.B39

polypeptide + H2O = peptides

647353, 647354, 647355

-

3.4.21.B40

polypeptide + H2O = peptides

647359, 647361, 647358

-

3.4.21.B41

polypeptide + H2O = peptides

647362

-

3.4.21.B42

polypeptide + H2O = peptides

647365

-

3.4.21.B43

polypeptide + H2O = peptides

647367

-

3.4.21.B45

polypeptide + H2O = peptides

647376

-

3.4.22.24

tyrosine aminotransferase + H2O = truncated tyrosine aminotransferase + peptide

-

-

3.4.22.25

protein + H2O = peptides

651248, 652619

-

3.4.22.29

cellular eukaryotic translation initiation factor eIF4GI + H2O = peptides

-

-

3.4.22.29

cellular eukaryotic translation initiation factor eIF4GII + H2O = peptides

-

-

3.4.22.29

2 entries

3.4.22.30

protein + H2O = peptides

649695, 649711, 649806, 649807, 649808, 649880, 652619, 651250

-

3.4.22.31

protein + H2O = peptides

649650, 649918

-

3.4.22.32

protein + H2O = peptides

650260, 650459, 651136, 651753, 652582, 653021, 653423

-

3.4.22.33

protein + H2O = peptides

650803

-

3.4.22.34

protein + H2O = peptides

650457, 651253, 651251, 653173, 649664, 650453, 650466, 651877, 651931, 654008, 651949, 650471, 650474

-

3.4.22.35

protein + H2O = peptides

649500, 651056, 653261, 653742, 653256

-

3.4.22.37

protein + H2O = peptides

638849, 650186, 650451, 650464, 650964, 653818, 651891

-

3.4.22.B67

Smt3-precursor + H2O = SMT3 + peptide

-

-

3.4.23.25

proproteinase A + H2O = pseudo-proteinaseA + peptide

-

-

3.4.23.B1

polypeptide + H2O = peptides

-

-

3.4.24.87

proteins + H2O = peptides

650102, 650710, 650712, 650714, 650715, 650717, 650725, 651439, 652431, 652481, 653678, 650709, 652191

-

3.4.24.B10

protein + H2O = peptides

649712, 652137, 653221, 652051, 653225, 649557, 651290, 651920, 652002, 651993, 652478

-

3.4.24.B10

proteins + H2O = peptides

651886

-

3.4.24.B10

2 entries

3.4.24.B11

proteins + H2O = peptides

651268, 651525, 652621, 638960, 649329, 649597, 652049, 652409, 651153, 651941, 395498, 651928

-

3.4.24.B12

proteins + H2O = peptides

651091, 652102, 652268, 651525, 395498, 651153

-

3.4.24.B14

protein + H2O = peptides

395498, 651958

-

3.4.24.B15

protein + H2O = peptides

650782, 649294, 649754, 652449, 395498, 649573, 649704, 652458, 649604, 651218

-

3.4.24.B16

protein + H2O = peptides

649501, 651616, 651625, 651880, 651900, 653278

-

3.4.24.B17

protein + H2O = peptides

650302, 649174, 649856, 650082, 651232, 651260, 651279, 651634, 651691, 651704, 652391, 652491, 652822, 653608, 653690, 651768, 651654, 653896, 649814, 653191, 651856, 650184, 651418,

-

3.4.24.B18

protein + H2O = peptides

650958, 395498, 653198, 651889, 649814, 650372

-

3.4.24.B19

protein + H2O = peptides

649814, 650958

-

3.4.24.B19

proteins + H2O = peptides

395498

-

3.4.24.B19

2 entries

3.4.24.B2

protein + H2O = peptides

651847, 650746

-

3.4.24.B20

protein + H2O = peptides

649814, 651855, 653478

-

3.4.24.B20

proteins + H2O = peptides

395498

-

3.4.24.B20

2 entries

3.4.24.B23

pro-sigmaK + H2O = sigmaK + peptide

-

-

3.4.24.B3

protein + H2O = peptides

649860, 651843, 651898, 653720, 652423, 395498, 649230, 652852, 651851, 651871, 653398

-

3.4.24.B4

protein + H2O = peptides

649335, 651876, 652045, 651954, 652827, 652829, 395498, 652802, 652774, 651854, 650906

-

3.4.24.B5

protein + H2O = peptides

651039, 651754, 652122, 395498

-

3.4.24.B6

proteins + H2O = peptides

651273, 652629, 649826, 651269, 652736, 651185, 395498

-

3.4.24.B7

proteins + H2O = peptides

652254, 652493, 652014, 649708, 650768

-

3.4.24.B8

proteins + H2O = peptides

650941, 653330, 653606, 395498, 649618

-

3.4.24.B9

proteins + H2O = peptides

649674, 650963, 651956, 651966, 644075, 649562, 651308, 653225, 653737, 395498, 649598

-

3.5.1.114

Nalpha-acetylated peptide + H2O = acetate + peptide

-

-

Substrate in Enzyme-catalyzed Reactions (36 results)

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Show Substrate (36 entries)

EC NUMBER

REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

2.3.1.255

acetyl-CoA + peptide = CoA + Nalpha-acetylpeptide

720453, 657745

-

2.3.1.255

acetyl-CoA + peptide = Nalpha-acetylpeptide + CoA

702871, 705613, 706924

-

2.3.1.255

2 entries

2.3.1.257

acetyl-CoA + peptide = CoA + Nalpha-acetylpeptide

720835

-

2.3.1.258

acetyl-CoA + peptide = CoA + Nalpha-acetylpeptide

719976, 720002

-

2.3.1.5

acetyl-CoA + peptide = CoA + Nalpha-acetylpeptide

487664

-

2.7.10.2

ATP + peptide = ADP + phospho-L-tyrosinyl-peptide

676750

-

2.7.11.12

ATP + a peptide = ADP + a phosphorylated peptide

675507

-

2.7.11.14

ATP + peptide = ADP + phosphopeptide

640716, 640730, 640706, 640709, 640717, 640727, 640703, 640701, 490997

-

2.7.11.15

ATP + peptide = ADP + phosphopeptide

645011, 645012, 640709

-

3.4.11.10

Peptides + H2O = ?

81170, 81171, 81172, 81173, 81174, 81175, 81176, 81177, 81178, 81179, 81180, 81181, 81182, 81183, 81184, 81185, 81186, 81187, 81189, 81190, 81188

-

3.4.11.10

peptides + H2O = N-terminal amino acid + peptide(n-1)

652573

-

3.4.11.10

2 entries

3.4.11.13

Peptides + H2O = ?

81193, 81194, 81195, 81196, 81197

-

3.4.11.16

Peptides + H2O = ?

643871, 643872, 643877, 643870, 643874

-

3.4.11.24

peptide + H2O = ?

649123, 651036, 651046, 651836, 652773, 652775, 653768, 653836, 651033, 651038

-

3.4.11.3

Peptides + H2O = ?

35907, 35919

-

3.4.17.B1

peptide + H2O = ?

649646, 651211, 651034

-

3.4.21.26

Peptides + H2O = ?

81344, 81340

-

3.4.21.80

Peptide + H2O = Hydrolyzed peptide + H2O

29755

-

3.4.21.B10

peptide + H2O = ?

691153

-

3.4.22.48

peptide + H2O = amino acids

643962, 643966, 643963

-

3.4.22.48

peptide + H2O = peptide proteolytically cleaved into fragments or single amino acids

643962, 643966, 643963

-

3.4.22.48

2 entries

3.4.22.B24

peptide + H2O = hydrolyzed peptide

395498

-

3.4.22.B25

peptide + H2O = hydrolyzed peptide

395498, 644012, 644024, 648088, 649063

-

3.4.22.B27

peptide + H2O = hydrolyzed peptide

395498, 648090, 648091, 644012

-

3.4.22.B28

peptide + H2O = hydrolyzed peptide

648093, 648094

-

3.4.22.B29

peptide + H2O = hydrolyzed peptide

395498

-

3.4.22.B30

peptide + H2O = hydrolyzed peptide

395498, 648105

-

3.4.22.B31

peptide + H2O = hydrolyzed peptide

395498

-

3.4.22.B32

peptide + H2O = hydrolyzed peptide

395498

-

3.4.22.B35

peptide + H2O = hydrolyzed peptide

395498

-

3.4.22.B36

peptide + H2O = hydrolyzed peptide

648415

-

3.4.22.B37

peptide + H2O = hydrolyzed peptide

395498

-

3.4.23.12

Peptides + H2O = ?

36777, 36778, 36773, 36774, 36771, 36772, 36775, 36776

-

3.4.23.21

Peptides + H2O = ?

30606, 30605, 30559, 30625

-

3.4.23.23

Peptides + H2O = Hydrolyzed peptides

30566, 30589, 30652, 30664, 30665, 30674, 30668, 30667

-

3.4.24.B7

peptide + H2O = ?

652303

-

Product in Enzyme-catalyzed Reactions (105 results)

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Show Product (105 entries)

EC NUMBER

REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

2.3.2.2

a (5-L-glutamyl)-peptide + an amino acid = a peptide + a 5-L-glutamyl amino acid

-

-

2.3.2.2

(5-L-glutamyl)-peptide + acceptor + H+ = peptide + 5-L-glutamyl amino acid

, 487903, 487956, 487970, 487962, 487968, 487972, 487930, 487954, 487943, 487944, 487966, 487952, 487951, 487959, 487967

-

2.3.2.2

(5-L-glutamyl)-peptide + an amino acid = peptide + 5-L-Glu-Xaa

-

-

2.3.2.2

(5-L-glutamyl)-peptide + an amino acid = peptide + a 5-L-glutamyl amino acid

-

-

3.1.1.29

peptidyl-tRNA + H2O = peptide + tRNA

-

-

3.1.1.29

peptidyl-tRNAL + H2O = peptide + tRNA

-

-

3.1.1.29

peptidyl-tRNALys + H2O = peptide + tRNALys

-

-

2.3.2.2

4 entries

3.1.1.29

3 entries

3.1.1.5

palmitoyl-peptide + H2O = palmitate + peptide

-

-

3.1.2.22

palmitoyl-peptide + H2O = palmitate + peptide

-

-

3.1.3.16

phosphorylated peptide + H2O = peptide + phosphate

-

-

3.4.11.1

L-amino acid-peptide + H2O = amino acid + peptide

-

-

3.4.11.18

L-Met-peptide + H2O = L-Met + peptide

-

-

3.4.11.18

Met-peptide + H2O = Met + peptide

-

-

3.4.11.18

2 entries

3.4.11.23

Xaa-peptide + H2O = Xaa + peptide

643878

-

3.4.11.5

L-prolyl-peptide + H2O = L-proline + peptide

-

-

3.4.11.6

L-Arg-peptide + H2O = L-Arg + peptide

-

-

3.4.11.6

L-Lys-peptide + H2O = L-Lys + peptide

-

-

3.4.11.7

L-Asp-peptide + H2O = L-Asp + peptide

-

-

3.4.11.7

L-Glu-peptide + H2O = L-Glu + peptide

-

-

3.4.11.6

2 entries

3.4.11.7

2 entries

3.4.11.9

L-prolyl-peptide + H2O = L-proline + peptide

-

-

3.4.17.B1

protein + H2O = peptides

649646, 651211, 651034

-

3.4.19.12

ubiquitinyl-peptide + H2O = ubiquitin + peptide

-

-

3.4.19.3

pyroglutamyl-peptide + H2O = pyroglutamate + peptide

652124

-

3.4.21.10

proacrosin + H2O = acrosin + peptide

-

-

3.4.21.102

pre-D1 protein + H2O = D1 protein + peptide

-

-

3.4.21.117

oxidized bovine insulin B chain + H2O = peptides + (Tyr)26

647345

-

3.4.21.117

polypeptide + H2O = peptides

647342, 647343, 647345, 647346, 647347, 647348, 647331, 647332, 647344, 647349

-

3.4.21.117

2 entries

3.4.21.118

polypeptide + H2O = peptides

647331, 647321, 647322, 647323, 647325, 647326, 647327, 647328, 647329, 647324, 647332

-

3.4.21.119

polypeptide + H2O = peptides

647369, 647370, 647371, 647372, 647373

-

3.4.21.19

human parathyroid hormone(13-34) + H2O = peptides

81322

-

3.4.21.20

factor VIII + H2O = factor VIIIa + peptide

-

-

3.4.21.20

factor VIIIa + H2O = factor VIII + peptide

-

-

3.4.21.20

RANTES 1-68 + H2O = RANTES 4-68 + peptide

-

-

3.4.21.20

3 entries

3.4.21.25

peptidyl-p-nitroanilide + H2O = p-nitroaniline + peptide

-

-

3.4.21.27

factor IX + H2O = factor IXa + peptide

, 652309, 36535

-

3.4.21.35

polypeptide + H2O = peptides

647332, 647361, 647483, 647485, 647486, 647487, 647488, 647497, 647498, 647500, 647501, 647502, 647503, 647506, 647508, 647509, 647510, 647512, 647513, 647514, 647519, 647522, 647523, 647531, 647536, 647537, 647540, 647542, 647331, 647480, 647482, 647494, 647495, 647496, 647504, 647505, 647530, 95367, 647481, 647484, 647491, 647492, 647499, 647517, 647511, 395498, 647515, 647489

-

3.4.21.62

porcine brain tubulin + H2O = peptides

-

-

3.4.21.75

peptidyl-7-amido-4-methyl-coumarin + H2O = 7-amino-4-methyl-coumarin + peptide

650437

-

3.4.21.77

polypeptide + H2O = peptides

647587, 647588, 647589, 647590, 647591, 647592, 647594, 647332

-

3.4.21.86

peptide-4-nitroanilide + H2O = peptide + 4-nitroaniline

-

-

3.4.21.89

intermediate of cytochrome c peroxidase + H2O = mature cytochrome c peroxidase + peptide

-

-

3.4.21.92

Arc-ssrA + H2O = peptides

-

-

3.4.21.B10

polypeptide + H2O = peptides

, 647332

-

3.4.21.B12

polypeptide + H2O = peptides

647338, 647333, 647339, 647332, 647334, 647335, 647336, 647337

-

3.4.21.B3

polypeptide + H2O = peptides

-

-

3.4.21.B39

polypeptide + H2O = peptides

647353, 647354, 647355

-

3.4.21.B40

polypeptide + H2O = peptides

647359, 647361, 647358

-

3.4.21.B41

polypeptide + H2O = peptides

647362

-

3.4.21.B42

polypeptide + H2O = peptides

647365

-

3.4.21.B43

polypeptide + H2O = peptides

647367

-

3.4.21.B45

polypeptide + H2O = peptides

647376

-

3.4.22.1

trypsinogen + H2O = trypsin + peptide

-

-

3.4.22.2

azocasein + H2O = azopeptide + peptides

-

-

3.4.22.24

tyrosine aminotransferase + H2O = truncated tyrosine aminotransferase + peptide

-

-

3.4.22.25

protein + H2O = peptides

651248, 652619

-

3.4.22.29

cellular eukaryotic translation initiation factor eIF4GI + H2O = peptides

-

-

3.4.22.29

cellular eukaryotic translation initiation factor eIF4GII + H2O = peptides

-

-

3.4.22.29

2 entries

3.4.22.30

protein + H2O = peptides

649695, 649711, 649806, 649807, 649808, 649880, 652619, 651250

-

3.4.22.31

protein + H2O = peptides

649650, 649918

-

3.4.22.32

protein + H2O = peptides

650260, 650459, 651136, 651753, 652582, 653021, 653423

-

3.4.22.33

protein + H2O = peptides

650803

-

3.4.22.34

protein + H2O = peptides

650457, 651253, 650474, 651251, 653173, 649664, 650453, 650466, 651877, 651931, 654008, 651949, 650471

-

3.4.22.35

complement factor C3 + H2O = peptides

653256

-

3.4.22.35

complement factor C9 + H2O = peptides

653256

-

3.4.22.35

fibronectin + H2O = peptides

653256

-

3.4.22.35

protein + H2O = peptides

649500, 651056, 653261, 653742, 653256

-

3.4.22.35

4 entries

3.4.22.37

protein + H2O = peptides

638849, 650186, 650451, 650464, 650964, 653818, 651891

-

3.4.22.B67

Smt3-precursor + H2O = SMT3 + peptide

-

-

3.4.22.B70

CrSUMO148 precursor + H2O = CrSUMO148 + peptide

-

-

3.4.22.B70

CrSUMO96 precursor + H2O = CrSUMO96 + peptide

-

-

3.4.22.B70

CrSUMO97 precursor + H2O = CrSUMO97 + peptide

-

-

3.4.22.B70

3 entries

3.4.23.25

proproteinase A + H2O = pseudo-proteinaseA + peptide

-

-

3.4.23.B1

polypeptide + H2O = peptides

-

-

3.4.24.33

Apolipoprotein A-I + H2O = Peptides

31207

-

3.4.24.33

Pancreatic ribonuclease + H2O = Peptides

31205

-

3.4.24.33

2 entries

3.4.24.87

proteins + H2O = peptides

650102, 650710, 650712, 650714, 650715, 650717, 650725, 651439, 652431, 652481, 653678, 650709, 652191

-

3.4.24.B10

protein + H2O = peptides

649712, 652137, 653221, 652051, 652478, 653225, 649557, 651290, 651886, 651920, 652002, 651993

-

3.4.24.B10

proteins + H2O = peptides

651886

-

3.4.24.B10

2 entries

3.4.24.B11

proteins + H2O = peptides

651268, 651525, 651928, 652621, 638960, 649329, 649597, 652049, 652409, 651153, 651941, 395498

-

3.4.24.B12

proteins + H2O = peptides

651091, 652102, 652268, 651525, 395498, 651153

-

3.4.24.B14

protein + H2O = peptides

395498, 651958

-

3.4.24.B15

protein + H2O = peptides

650782, 649294, 649604, 649573, 649704, 649754, 651218, 652458, 652449, 395498

-

3.4.24.B16

protein + H2O = peptides

649501, 651616, 651625, 651880, 651900, 653278

-

3.4.24.B17

casein + H2O = peptides

653690

-

3.4.24.B17

largely unfolded alpha-lactalbumin + H2O = peptides

651768

-

3.4.24.B17

protein + H2O = peptides

650302, 649174, 649856, 650082, 650184, 651232, 651260, 651279, 651634, 651691, 651704, 651856, 652391, 652491, 652822, 653608, 653690, 653896, 651418, 651768, 649814, 653191, 651654,

-

3.4.24.B17

protein sigma32 + H2O = peptides

650184

-

3.4.24.B17

unfolded alpha-casein + H2O = peptides

651768

-

3.4.24.B17

unfolded pepsin + H2O = peptides

651768

-

3.4.24.B17

6 entries

3.4.24.B18

protein + H2O = peptides

650958, 651889, 395498, 650372, 649814, 653198

-

3.4.24.B19

protein + H2O = peptides

649814, 650958

-

3.4.24.B19

proteins + H2O = peptides

395498

-

3.4.24.B19

2 entries

3.4.24.B2

protein + H2O = peptides

650746, 651847

-

3.4.24.B20

protein + H2O = peptides

651855, 653460, 653478, 649814

-

3.4.24.B20

proteins + H2O = peptides

395498

-

3.4.24.B20

2 entries

3.4.24.B23

pro-sigmaK + H2O = sigmaK + peptide

-

-

3.4.24.B3

protein + H2O = peptides

649860, 651843, 651851, 651898, 653398, 653720, 651871, 652423, 395498, 649230, 652852

-

3.4.24.B4

protein + H2O = peptides

649335, 650906, 651854, 651876, 652045, 651954, 652774, 652827, 652829, 395498, 652802

-

3.4.24.B5

protein + H2O = peptides

651039, 651754, 652122, 395498

-

3.4.24.B6

endostatin + H2O = peptides

651273

-

3.4.24.B6

proteins + H2O = peptides

651273, 652629, 649826, 651269, 652736, 651185, 395498

-

3.4.24.B6

2 entries

3.4.24.B7

proteins + H2O = peptides

652254, 652493, 652014, 649708, 650768

-

3.4.24.B8

proteins + H2O = peptides

649618, 650941, 653330, 653606, 395498

-

3.4.24.B9

proteins + H2O = peptides

649674, 650963, 651956, 651966, 644075, 649562, 651308, 653225, 653737, 395498, 649598

-

3.5.1.114

Nalpha-acetylated peptide + H2O = acetate + peptide

-

-

Inhibitor in Enzyme-catalyzed Reactions (15 results)

top print hide

Show Inhibitors (15 entries)

EC NUMBER

COMMENTARY

LITERATURE

ENZYME 3D STRUCTURE

1.14.17.3

especially those with COOH-terminal glycine residues

438572

-

1.97.1.4

peptides homologous to the Gly734 site of pyruvate formate-lyase that are active as substrates

14933

-

2.7.11.15

synthetic peptides derived from the receptor intracellular loop inhibit

645023

-

2.7.11.15

synthetic peptides from a variety of intracellular regions of beta2-AR specifically inhibit phosphorylation of the intact receptor, but not of peptide substrates

640709

-

2.7.11.15

2 entries

3.4.14.5

diacylhydroxylamine derivatives of Xaa-Pro or Xaa-Ala peptides. Different oligopeptides with N-terminal Xaa-Pro-sequences

36261

-

3.4.15.1

more angiotensin I converting enzyme-inhibitory peptides are present in hydrolyzed wet-milled corn germ compared to hydrolyzed dry-milled germ

680328

-

3.4.15.1

purified from sunflower hydrolysate

680284

-

3.4.15.1

purified from sunflower hydrolysate or rapeseed hydrolysate

680284

-

3.4.15.1

3 entries

3.4.19.12

containing either of the cleavage site sequence found in ubiquitin polymers, but not unrelated peptides

646094

-

3.4.22.49

acyloxymethyl ketone derivative of human SCC1 cleavage site peptide, chloromethyl ketone derivatives of the yeast Scc1 cleavage site

638865

-

3.4.23.1

29 amino acid peptide liberated in activation of pepsinogen

35005

-

3.4.24.26

containing the hydroxamic acid, N-hydroxypeptide and thiol functional groups

31113, 31116

-

3.5.1.5

TFLPQPRCSALLRYLSEDGVIVPS and YDFYWW, no inhibition of the enzyme from Bacillus pasteurii and Canavalia ensiformis

209168

-

4.1.2.13

-

4956

-

5.3.4.1

study of the inhibition of enzyme catalyzed reduction of insulin by GSH by peptides of various length and amino acid composition

3069

-

Enzyme Kinetic Parameters

k_cat Value (Turnover Number) (1 result)

top print hide

Show Turnover Number (1 entry)

EC NUMBER

TURNOVER NUMBER [1/S]

TURNOVER NUMBER MAXIMUM [1/S]

COMMENTARY

LITERATURE

3.4.11.10

67

-

-

652573

K_M Value (4 results)

top print hide

Show KM Value (4 entries)

EC NUMBER

KM VALUE [MM]

KM VALUE MAXIMUM [MM]

COMMENTARY

LITERATURE

2.7.11.15

0.9

1.3

acid-rich synthetic peptides

640709

2.7.11.15

1.5

4.8

synthetic peptides containing a single Glu-residue

640709

2.7.11.19

0.2

2.3

from phosphorylase b, synthetic

492125

2.7.11.19

0.7

3.5

from glycogen synthase, synthetic

492125

2.7.11.15

2 entries

2.7.11.19

2 entries

References & Links

Literature References (416)

top print hide

Show Reference (416 entries)

BRENDA REFERENCE ID

PUBMED ID

TITLE

YEAR

AUTHORS

JOURNAL

VOLUME

PAGES

3069

2036365

Effect of protein and peptide inhibitors on the activity of protein disulfide isomerase

1991

Morjana, N.A.; Gilbert, H.F.

Biochemistry

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4985-4990

4956

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Expression, purification, biochemical characterization and inhibition of recombinant Plasmodium falciparum aldolase

1990

Döbeli, H.; Trzeciak, A.; Gillessen, A.; Matile, H.; Srivastava, I.K.; Perrin, L.H.; Jakob, P.E.; Certa, U.

Mol. Biochem. Parasitol.

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14933

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Adenosylmethionine-dependent synthesis of the glycyl radical in pyruvate formate-lyase by abstraction of the glycine C-2 pro-S hydrogen atom

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Active centers of alpha-chymotrypsin and of Streptomyces griseus proteases 1 and 3. S2-P2 enzyme-substrate interactions

1980

Bauer, C.A.

Eur. J. Biochem.

105

565-570

30559

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Comparative study on the specificities of several fungal aspartic and acidic proteinases towards the tetradecapeptide of a renin substrate

1988

Majima, E.; Oda, K.; Murao, S.; Ichishima, E.

Agric. Biol. Chem.

52

787-793

30566

4581238

Comparative specificity of microbial acid proteinases for synthetic peptides. 3. Relationship with their trypsinogen activating ability

1973

Morihara, K.; Oka, T.

Arch. Biochem. Biophys.

157

561-572

30589

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A systematic series of synthetic chromophoric substrates for aspartic proteinases

1986

Dunn, B.M.; Jimenez, M.; Parten, B.F.; Valler, M.J.; Rolph, C.E.; Kay, J.

Biochem. J.

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30605

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Mold proteases. II. Substrate specificity of acid protease of Rhizopus chinensis

1969

Tsuru, D.; Hattori, A.; Tsuji, H.; Yamamoto, T.; Fukumoto, J.

Agric. Biol. Chem.

33

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30606

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Isolation of a protease from a Rhizopus product

1971

Kurono, Y.; Chidimatsu, M.; Korikoshi, K.; Ikeda, Y.

Agric. Biol. Chem.

35

1668-1675

30625

7613467

Engineering the substrate specificity of rhizopuspepsin: the role of Asp 77 of fungal aspartic proteinases in facilitating the cleavage of oligopeptide substrates with lysine in P1

1995

Lowther, W.T.; Majer, P.; Dunn, B.M.

Protein Sci.

4

689-702

30652

6768392

Kinetic studies on the action of Mucor pusillus, Mucor miehei acid proteases and chymosins A and B on a synthetic chromophoric hexapeptide

1980

Martin, P.; Raymond, M.N.; Bricas, E.; Dumas, B.R.

Biochim. Biophys. Acta

612

410-420

30664

4578121

Comparative specificity of microbial acid proteinases for synthetic peptides. II. Effect of secondary interaction

1973

Oka, T.; Morihara, K.

Arch. Biochem. Biophys.

156

552-559

30665

4578120

Comparative specificity of microbial acid proteinases for synthetic peptides. I. Primary specificity

1973

Oka, T.; Morihara, K.

Arch. Biochem. Biophys.

156

543-551

30667

4573298

Bond specificity, active site and milk clotting mechanism of the Mucor miehei protease

1972

Sternberg, M.

Biochim. Biophys. Acta

285

383-392

30668

-

Milk-clotting enzyme for Mucor pusillus var Lindt

1970

Arima, K.; Yu, J.; Iwasaki, S.

Methods Enzymol.

19

446-459

30674

5277065

The comparative specificity of acid proteinases

1971

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

Proc. Natl. Acad. Sci. USA

68

257-259

31113

6767718

Pseudomonas aeruginosa elastase. Development of a new substrate, inhibitors, and an affinity ligand

1980

Nishino, N.; Powers, J.C.

J. Biol. Chem.

255

3482-3486

31116

7674924

Pseudolysin and other pathogen endopeptidases of thermolysin family

1995

Morihara, K.

Methods Enzymol.

248

242-253

31205

7188696

Substrate specificity of a proteolytic enzyme isolated from a mutant of Pseudomonas fragi

1980

Drapeau, G.R.

J. Biol. Chem.

255

839-840

31207

1981672

Relaxed specificity of endoproteinase Asp-N: this enzyme cleaves at peptide bonds N-terminal to glutamate as well as aspartate and cysteic acid residues

1990

Tetaz, T.; Morrison, J.R.; Andreou, J.; Fidge, N.H.

Biochem. Int.

22

561-566

35005

-

Pepsin

1971

Fruton, J.S.

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

3

119-164

35907

6041057

Biochemical studies on oxytocin and oxytocinase

1967

Sjoeholm, I.

Acta Pharm. Suec.

4

81-96

35919

7889600

Evaluation of enzyme inhibitors of cystinyl aminopeptidase and application to the measurement of immunoreactive atrial natriuretic peptide in human pregnancy

1994

Irons, D.W.; Davison, J.M.; Baylis, P.H.

Clin. Chim. Acta

231

185-191

36261

1678607

Dipeptidyl peptidase IV in the immune system. Effects of specific enzyme inhibitors on activity of dipeptidyl peptidase IV and proliferation of human lymphocytes

1991

Schön, E.; Born, I.; Demuth, H.U.; Faust, J.; Neubert, K.; Steinmetzer, T.; Barth, A.; Ansorge, S.

Biol. Chem. Hoppe-Seyler

372

305-311

36535

4473201

The mechanism of activation of bovine factor IX (Christmas factor) by bovine factor XIa (activated plasma thromboplastin antecedent)

1974

Fujikawa, K.; Legaz, M.E.; Kato, H.; Davie, E.W.

Biochemistry

13

4508-4516

36771

5354017

Acid protease in Nepenthes. II. Study on the specificity of nepenthesin

1969

Amagase, S.; Nakayama, S.; Tsugita, A.

J. Biochem.

66

431-439

36772

24549466

Reinigung der Proteinase aus Nepenthes-Kannensaft

1967

Steckelberg, R.; Luettge, U.; Weigl, J.

Planta

76

238-241

36773

5069751

Digestive enzymes in insectivorous plants. III. Acid proteases in the genus Nepenthes and Drosera peltata

1972

Amagase, S.

J. Biochem.

72

73-81

36774

4634982

Digestive enzymes in insectivorous plants. IV. Enzymatic digestion of insects by Nepenthes secretion and Drosera peltata extract: proteolytic and chitinolytic activities

1972

Amagase, S.; Mori, M.; Nakayama, S.

J. Biochem.

72

765-767

36775

11946525

Enzymes from arnivorous plants (Nepenthes). Isolation of the protease nepenthacin

1972

Jentsch, J.

FEBS Lett.

21

273-276

36776

2666423

Purification of the decomposing enzyme from Nepenthes alata against glycophorin B of human red blood cells by high-performance liquid chromatography

1989

Kamesaki, T.; Kajii, E.; Ikemoto, S.

J. Chromatogr.

489

384-389

36777

4436292

Specific inhibition of acid proteases from brain, kidney, skeletal muscle, and insectivorous plants by diazoacetyl-DL-norleucine methyl ester and by pepstatin

1974

Takahshi, K.; Chang, W.J.; Ko, J.S.

J. Biochem.

76

897-899

36778

9561252

Acid proteinase from Nepenthes distillatoria (Badura)

1998

Brodelius, P.E.; Cordeiro, M.; Mercke, P.; Domingos, A.; Clemente, A.; Pais, M.S.

Adv. Exp. Med. Biol.

436

453-458

81170

4026862

A transition-state-analog inhibitor influences zinc-binding by Aeromonas aminopeptidase

1985

Baker, J.O.; Prescott, J.M.

Biochem. Biophys. Res. Commun.

130

1154-1160

81171

2865258

The slow, tight binding of bestatin and amastatin to aminopeptidases

1985

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

J. Biol. Chem.

260

13154-13162

81172

4074699

Spectral and kinetic studies of metal-substituted Aeromonas aminopeptidase: nonidentical, interacting metal-binding sites

1985

Prescott, J.M.; Wagner, F.W.; Holmquist, B.; Vallee, B.L.

Biochemistry

24

5350-5356

81173

6643439

Stereospecificity of amino acid hydroxamate inhibition of aminopeptidases

1983

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

J. Biol. Chem.

258

13517-13521

81174

6882446

One hundred fold increased activity of Aeromonas aminopeptidase by sequential substitutions with Ni(II) or Cu(II) followed by zinc

1983

Prescott, J.M.; Wagner, F.W.; Holmquist, B.; Vallee, B.L.

Biochem. Biophys. Res. Commun.

114

646-652

81175

6860652

Hydroxamates and aliphatic boronic acids: marker inhibitors for aminopeptidase

1983

Baker, J.O.; Wilkes, S.H.; Bayliss, M.E.; Prescott, J.M.

Biochemistry

22

2098-2103

81176

1012016

Aeromonas aminopeptidase

1976

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

Methods Enzymol.

45

530-543

81177

4441102

Kinetics of inhibition of Aeromonas aminopeptidase by leucine methyl ketone derivatives

1974

Kettner, C.; Glover, G.I.; Prescott, J.M.

Arch. Biochem. Biophys.

165

739-743

81178

4831337

The purification of Aeromonas aminopeptidase by affinity chromatography

1974

Kettner, C.; Rodriguez-Absi, J.; Glover, G.I.; Prescott, J.M.

Arch. Biochem. Biophys.

162

56-63

81179

5010066

Specificity of Aeromonas aminopeptidase toward amino acid amides and dipeptides

1972

Wagner, F.W.; Wilkes, S.H.; Prescott, J.M.

J. Biol. Chem.

247

1208-1210

81180

5102149

Aeromonas aminopeptidase. Improved isolation and some physical properties

1971

Prescott, J.M.; Wilkes, S.H.; Wagner, F.W.; Wilson, K.J.

J. Biol. Chem.

246

1756-1764

81181

4961737

Aeromonas aminopeptidase: purification and some general properties

1966

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

Arch. Biochem. Biophys.

117

328-336

81182

7173208

Chemical modification of Aeromonas aminopeptidase. Evidence for the involvement of tyrosyl and carboxyl groups in the activity of the enzyme

1982

Maekinen, K.K.; Maekinen, P.L.; Wilkes, S.H.; Bayliss, M.E.; Prescott, J.M.

Eur. J. Biochem.

128

257-265

81183

7056743

Photochemical inactivation of Aeromonas aminopeptidase by 2,3-butanedione

1982

Maekinen, K.K.; Maekinen, P.L.; Wilkes, S.H.; Bayliss, M.E.; Prescott, J.M.

J. Biol. Chem.

257

1765-1772

81184

4351847

Specificity of aeromonas aminopeptidase toward oligopeptides and polypeptides

1973

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

Eur. J. Biochem.

34

459-466

81185

1550363

Rapid purification of the Aeromonas proteolytica aminopeptidase: crystallization and preliminary X-ray data

1992

Schalk, C.; Remy, J.M.; Chevrier, B.; Moras, D.; Tarnus, C.

Arch. Biochem. Biophys.

294

91-97

81186

9245416

Spectroscopically distinct cobalt(II) sites in heterodimetallic forms of the aminopeptidase from Aeromonas proteolytica: characterization of substrate binding

1997

Bennett, B.; Holz, R.C.

Biochemistry

36

9837-9846

81187

8647077

The structure of the Aeromonas proteolytica aminopeptidase complexed with a hydroxamate inhibitor. Involvement in catalysis of Glu151 and two zinc ions of the co-catalytic unit

1996

Chevrier, B.; D'Orchymont, H.; Schalk, C.; Moras, D.

Eur. J. Biochem.

237

393-398

81188

10413478

1-Butaneboronic acid binding to Aeromonas proteolytica aminopeptidase: a case of arrested development

1999

De Paola, C.C.; Bennett, B.; Holz, R.C.; Ringe, D.; Petsko, G.A.

Biochemistry

38

9048-9053

81189

10471294

Inhibition of the aminopeptidase from Aeromonas proteolytica by aliphatic alcohols. Characterization of the hydrophobic substrate recognition site

1999

Ustynyuk, L.; Bennett, B.; Edwards, T.; Holz, R.C.

Biochemistry

38

11433-11439

81190

10569943

Slow-binding inhibition of the aminopeptidase from Aeromonas proteolytica by peptide thiols: synthesis and spectroscopic characterization

1999

Huntington, K.M.; Bienvenue, D.L.; Wei, Y.; Bennett, B.; Holz, R.C.; Pei, D.

Biochemistry

38

15587-15596

81193

6477932

Soluble and immobilized clostridial aminopeptidase and aminopeptidase P as metal-requiring enzymes

1984

Fleminger, G.; Yaron, A.

Biochim. Biophys. Acta

789

245-256

81194

6830820

Sequential hydrolysis of proline-containing peptides with immobilized aminopeptidases

1983

Fleminger, G.; Yaron, A.

Biochim. Biophys. Acta

743

437-446

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

81322

1429718

Purification, characterization, cloning, and expression of a glutamic acid-specific protease from Bacillus licheniformis ATCC 14580

1992

Kakudo, S.; Kikuchi, N.; Kitadokoro, K.; Fujiwaera, T.; Nakamura, E.; Okamoto, H.; Shin, M.; Tamaki, M.; Teraoka, H.; Tsuzuki, H.; Yoshida, N.

J. Biol. Chem.

267

23782-23788

81340

3480758

Rapid degradation of D- and L-succinimide-containing peptides by a post-proline endopeptidase from human erythrocytes

1987

Momand, J.; Clarke, S.

Biochemistry

26

7798-7805

81344

2651143

Involvement of prolyl endopeptidase in ascidian fertilization

1989

Yokosawa, H.; Nishikata, M.; Ishii, S.

Experientia

45

381-383

95367

10615004

Human plasma kallikrein and tissue kallikrein binding to a substrate based on the reactive site of a factor Xa inhibitor isolates from Bauhinia ungulata seeds

1999

Oliva, M.L.V.; Andrade, S.; Batista, I.F.C.; Sampaio, M.U.; Juliano, M.; Fritz, H.; Auerswald, E.A.; Sampaio, C.A.M.

Immunopharmacology

45

145-149

209168

10411639

New inhibitors of Helicobacter pylori urease holoenzyme selected from phage-displayed peptide libraries

1999

Houimel, M.; Mach, J.P.; Corthesy-Theulaz, I.; Fisch, I.

Eur. J. Biochem.

262

774-780

395498

12520024

The SWISS-PROT protein knowledgebase and its supplement TrEMBL

2003

Boeckmann, B.; Bairoch, A.; Apweiler, R.; Blatter, M.C.; Estreicher, A.; Gasteiger, E.; Martin M.J.; Michoud, K.; O'Donovan, C.; Phan, I.; Pilbout, S.; Schneider, M.

Nucleic Acids Res.

31

365-370

438572

6725255

Characterization of a peptide alpha-amidation activity from rat anterior pituitary

1984

Glembotski, C.C.; Eipper, B.A.; Mains, R.E.

J. Biol. Chem.

259

6385-6392

487664

11393533

Identification of single-nucleotide polymorphisms (SNPs) of human N-acetyltransferase genes NAT1, NAT2, AANAT, ARD1, and L1CAM in the Japanese population

2001

Sekine, A.; Saito, S.; Iida, A.; Mitsunobu, Y.; Higuchi, S.; Harigae, S.; Nakamura, Y.

Hum. Genet.

46

314-319

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

487930

2868391

gamma-Glutamyl transpeptidase: kinetics and mechanism

1985

Allison, D.

Methods Enzymol.

113

419-437

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

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Characterization of matrix metalloproteinase-26, a novel metalloproteinase widely expressed in cancer cells of epithelial origin

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Effects of the quality of the P2-S2 hydrophobic contacts on the catalytic activities of papain, caricain and ficin and their generation by electrostatic switches

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Evidence that the carboxy groups of Asp158 in papain and caricain have abnormally low pKa values and thus do not contribute the key ionizations with pKa 4 that generate catalytic competence

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Biochem. Soc. Trans.

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The kinetically influential ionizations of caricain D158N revealed by using 4,4'-dipyrimidyl disulfide as a reactivity probe

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Identification and structural and functional characterization of human enamelysin (MMP-20)

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Self-processing of FtsH and its implication for the cleavage specificity of this protease

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Biochemistry

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Role of the S1' subsite glutamine 215 in activity and specificity of stromelysin-3 by site-directed mutagenesis

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Biochemistry

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Estimating the degree of expansion in the transition state for protein unfolding: analysis of the pH dependence of the rate constant for caricain denaturation

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Biochemistry

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Mutagenesis and kinetic studies of a plant cysteine proteinase with an unusual arrangement of acidic amino acids in and around the active site

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Biochemistry

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Biochemistry

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Processing of von Willebrand Factor by ADAMTS-13

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Biochemistry

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Coupled kinetics of ATP and peptide hydrolysis by Escherichia coli FtsH protease

2003

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Biochemistry

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Characterization of the specificity of arginine-specific gingipains from Porphyromonas gingivalis reveals active site differences between different forms of the enzymes

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Biochemistry

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Guanidine hydrochloride denaturation of glycosylated and deglycosylated stem bromelain

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Structural and functional studies on an FtsH inhibitor from Bacillus subtilis

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Biochim. Biophys. Acta

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Membrane protein degradation by AAA proteases in mitochondria

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Biochim. Biophys. Acta

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Activation of progelatinase A by mammalian lugumain, a recently discovered cysteine proteinase

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Biol. Chem.

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Structure-function relationship of bromelain isoinhibitors from pineapple stem

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Inhibition f arginie gingipains (RgpB and HRgpA) with benzamidine inhibitors: zinc increases inhibitory potency

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Inhibition of mammalian legumain by Michael acceptors and AzaAsn-halomethylketones

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