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Ligand Tyr-Gly-Gly

Basic Ligand Information

Molecular Structure

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Roles as Enzyme Ligand

Substrate in Enzyme-catalyzed Reactions (3 results)

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Show Substrate (3 entries)

EC NUMBER

REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

1.14.18.1

L-Tyr-Gly-Gly + O2 = ?

697659

-

3.4.11.4

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

649359

-

3.4.15.1

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

81273

-

Product in Enzyme-catalyzed Reactions (14 results)

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Show Product (14 entries)

EC NUMBER

REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

3.4.14.9

YGGFLRKYP + H2O = YGG + FLRKYP

647183

-

3.4.15.1

Leu5-enkephalin + H2O = Tyr-Gly-Gly + Phe-Leu

0

-

3.4.15.1

Met5-enkephalin + H2O = Tyr-Gly-Gly + Phe-Met

0

-

3.4.15.1

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

650873

-

3.4.15.1

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

650873

-

3.4.15.1

4 entries

3.4.24.11

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

0

-

3.4.24.42

Met-enkephalin + H2O = Tyr-Gly-Gly + Phe-Met

0

-

3.4.24.48

Met-enkephalin + H2O = Tyr-Gly-Gly + Phe-Met

36970

-

3.4.24.77

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

0

-

3.4.24.77

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

0

-

3.4.24.B14

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

0

-

3.4.24.B14

Tyr-Gly-Gly-Phe-Leu-NH2 + H2O = Tyr-Gly-Gly + Phe-Leu-NH2

0

-

3.4.24.B14

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

0

-

3.4.24.B14

Tyr-Gly-Gly-Phe-Met-NH2 + H2O = Tyr-Gly-Gly + Phe-Met-NH2

0

-

3.4.24.77

2 entries

3.4.24.B14

4 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

1.14.18.1

3.2

-

in 0.1M sodium phosphate buffer (pH 7.0) at 25°C

697659

1.14.18.1

4

-

in 0.1M sodium phosphate buffer (pH 7.0) at 25°C

697659

1.14.18.1

2 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

1.14.18.1

0.21

-

in 0.1 M sodium phosphate buffer (pH 7.0) at 25°C

697659

1.14.18.1

6

-

in 0.1M sodium phosphate buffer (pH 7.0) at 25°C

697659

1.14.18.1

2 entries

References & Links

Literature References (6)

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Show Reference (6 entries)

BRENDA REFERENCE ID

PUBMED ID

TITLE

YEAR

AUTHORS

JOURNAL

VOLUME

PAGES

36970

2949699

Biochemical characterization of hemorrhagic toxins with fibrinogenase activity isolated from Crotalus ruber ruber venom

1987

Mori, N.; Nikali, T.; Sugihara, H.; Tu, A.T.

Arch. Biochem. Biophys.

253

108-121

81273

2990346

Enkephalin-degrading dipeptidyl carboxypeptidase in guinea pig serum: its properties and action on bioactive peptides

1985

Kase, R.; Hazato, T.; Shimamura, M.; Kiuchi, Y.; Katayama, T.

Arch. Biochem. Biophys.

240

330-336

647183

11843185

Rat tripeptidyl peptidase I: molecular cloning, functional expression, tissue localization and enzymatic characterization

2001

Du, P.G.; Kato, S.; Li, Y.H.; Maeda, T.; Yamane, T.; Yamamoto, S.; Fujiwara, M.; Yamamoto, Y.; Nishi, K.; Ohkubo, I.

Biol. Chem.

382

1715-1725

649359

10653753

Purification and molecular characterization of a tripeptidase (PepT) from Lactobacillus helveticus

2000

Savijoki, K.; Palva, A.

Appl. Environ. Microbiol.

66

794-800

650873

10825662

Purification and characterization of a dipeptidyl carboxypeptidase from the polychaete Neanthes virens resembling angiotensin I converting enzyme

2000

Kawamura, T.; Oda, T.; Muramatsu, T.

Comp. Biochem. Physiol. B

126

29-37

697659

-

Comparison of substrate specificity of tyrosinases from Trichoderma reesei and Agaricus bisporus

2009

Selinheimo, E.; Gasparetti, C.; Mattinen, M.; Steffensen, C.; Buchert, J.; Kruus, K.

Enzyme Microb. Technol.

44

1-10

Links to other databases for Tyr-Gly-Gly

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Show Links (1 entry)

ChEBI

PubChem