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Ligand Z-Gly-Pro-Leu-Gly-Pro

Basic Ligand Information

Molecular Structure

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Roles as Enzyme Ligand

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

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Show Natural Substrate (1 entry)

EC NUMBER

PROVEN IN VIVO REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

3.4.22.B60

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

718252

-

Substrate in Enzyme-catalyzed Reactions (10 results)

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Show Substrate (10 entries)

EC NUMBER

REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

3.4.14.5

benzyloxycarbonyl-Gly-Pro-Leu-Gly-Pro + H2O = Leu-Gly-Pro + ?

36242

-

3.4.16.5

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

679935

-

3.4.21.26

Benzyloxycarbonyl-Gly-Pro-Leu-Gly-Pro + H2O = Benzyloxycarbonyl-Gly-Pro + Leu-Gly-Pro

653873

-

3.4.21.62

Carboxybenzoyl-Gly-Pro-Leu-Gly-Pro-OH + H2O = Carboxybenzoyl-Gly-Pro-Leu + Gly-Pro-OH

29427

-

3.4.21.65

Benzyloxycarbonyl-Gly-Pro-Leu-Gly-Pro + H2O = ?

29530

-

3.4.22.B60

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

718252

-

3.4.22.B62

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

718252

-

3.4.24.3

carbobenzoxy-Gly-Pro-Leu-Gly-Pro + H2O = carbobenzoxy-Gly-Pro-Leu + Gly-Pro

37101, 37089, 37092

-

3.4.24.53

Benzyloxycarbonyl-Gly-Pro-Leu-Gly-Pro + H2O = Benzyloxycarbonyl-Gly-Pro + Leu-Gly-Pro

31297

-

3.4.24.B2

N-carboxylbenzoyl-Gly-Pro-Leu-Gly-Pro + H2O = ?

667271

-

Enzyme Kinetic Parameters

k_cat Value (Turnover Number) (3 results)

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Show Turnover Number (3 entries)

EC NUMBER

TURNOVER NUMBER [1/S]

TURNOVER NUMBER MAXIMUM [1/S]

COMMENTARY

LITERATURE

3.4.21.26

0.4

-

enzyme from kidney

653873

3.4.21.26

12.4

-

-

653873

3.4.21.26

53.3

-

enzyme from kidney

653873

3.4.21.26

3 entries

K_M Value (2 results)

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Show KM Value (2 entries)

EC NUMBER

KM VALUE [MM]

KM VALUE MAXIMUM [MM]

COMMENTARY

LITERATURE

3.4.21.26

0.68

-

enzyme from kidney

653873

3.4.24.53

22

-

-

31297

References & Links

Literature References (11)

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Show Reference (11 entries)

BRENDA REFERENCE ID

PUBMED ID

TITLE

YEAR

AUTHORS

JOURNAL

VOLUME

PAGES

29427

-

Subtilisins: primary structure, chemical and physical properties

1971

Markland, F.S.; Smith, E.L.

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

3

561-608

29530

3173

The substrate specificity of thermomycolase, an extracellular serine proteinase from the thermophilic fungus Malbranchea pulchella var. sulfurea

1975

Stevenson, K.J.; Gaucher, G.M.

Biochem. J.

151

527-542

31297

4984550

Purification and characterization of a proteinase in the venom of Trimeresurus flavoviridis. Complete separation of the enzyme from hemorrhagic activity

1970

Takahashi, T.; Ohsaka, A.

Biochim. Biophys. Acta

198

293-307

36242

962853

Dipeptidyl peptidase IV, a kidney brush-border serine peptidase

1976

Kenny, A.J.; Booth, A.G.; George, S.G.; Ingram, J.; Kershaw, D.; Wood, E.J.; Young, A.R.

Biochem. J.

155

169-182

37089

-

Bacterial collagenases

1982

Peterkofsky, B.

Methods Enzymol.

82

453-471

37092

14240635

Multiplicity of Clostridium histolyticum collagenases

1964

Mandl, I.; Keller, S.; Manahan, J.

Biochemistry

3

1737-1741

37101

-

The isolation of collagenase and its enzymological and physico-chemical proterties

1973

Hanada, K.; Mizutani, T.; Yamagishi, M.; Tsuji, H.; Misaki, T.; Sawada, J.

Agric. Biol. Chem.

37

1771-1781

653873

-

Proline-specific endopeptidases

2003

Besedin, D.V.; Rudenskaya, G.N.

Russ. J. Bioorg. Chem.

29

1-17

667271

16391147

Characterization of a novel PepF-like oligopeptidase secreted by Bacillus amyloliquefaciens 23-7A

2006

Chao, S.H.; Cheng, T.H.; Shaw, C.Y.; Lee, M.H.; Hsu, Y.H.; Tsai, Y.C.

Appl. Environ. Microbiol.

72

968-971

679935

100101624

Purification of serine carboxypeptidase from the hepatopancreas of Japanese common squid Todarodes pacificus and its application for elimination of bitterness from bitter peptides

2007

Komai, T.; Kawabata, C.; Tojo, H.; Gocho, S.; Ichishima, E.

Fish. Sci.

73

404-411

718252

21483711

Collagenolytic activities of the major secreted cathepsin L peptidases involved in the virulence of the helminth pathogen, Fasciola hepatica

2011

Robinson, M.W.; Corvo, I.; Jones, P.M.; George, A.M.; Padula, M.P.; To, J.; Cancela, M.; Rinaldi, G.; Tort, J.F.; Roche, L.; Dalton, J.P.

PLoS Negl. Trop. Dis.

5

e1012

Links to other databases for Z-Gly-Pro-Leu-Gly-Pro

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Show Links (1 entry)

ChEBI

PubChem