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Ligand Ala-Leu

Basic Ligand Information

Molecular Structure

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Roles as Enzyme Ligand

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

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Show Natural Substrate (2 entries)

EC NUMBER

PROVEN IN VIVO REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

3.4.11.1

Ala-Leu + H2O = Ala + Leu

643878

-

3.4.11.23

Ala-Leu + H2O = Ala + Leu

643878

-

Substrate in Enzyme-catalyzed Reactions (13 results)

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Show Substrate (13 entries)

EC NUMBER

REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

3.4.11.1

Ala-Leu + H2O = Ala + Leu

643878, 651057

-

3.4.11.1

L-Ala-L-Leu + H2O = L-Ala + L-Leu

651119

-

3.4.11.1

2 entries

3.4.11.14

Ala-Leu + H2O = Ala + Leu

647031

-

3.4.11.22

L-Ala-L-Leu + H2O = L-Ala + L-Leu

28298

-

3.4.11.23

Ala-Leu + H2O = Ala + Leu

643878

-

3.4.13.12

Ala-Leu + H2O = Ala + Leu

36096

-

3.4.13.18

Ala-Leu + H2O = Ala + Leu

137178, 137179, 137176, 137184, 137189

-

3.4.13.19

Ala-Leu + H2O = Ala + Leu

677698

-

3.4.13.20

Ala-Leu + H2O = Ala + Leu

647116

-

3.4.22.3

benzoyl-Arg-ethyl ester + Ala-Leu-OH = ?

95731

-

3.4.24.54

Ala-Leu + H2O = ?

668856

-

3.4.24.54

Ala-Leu + H2O = Alanine + leucine

31301

-

3.4.24.54

2 entries

5.1.1.20

L-Ala-L-Leu = L-Ala-D-Leu

729191

-

Product in Enzyme-catalyzed Reactions (22 results)

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Show Product (22 entries)

EC NUMBER

REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

3.4.14.1

Ala-Leu-NH2 + H2O = Ala-Leu + NH3

0

-

3.4.15.1

benzoyl-Gly-Ala-Leu + H2O = benzoyl-Gly + Ala-Leu

0

-

3.4.16.5

FVNQHLCGSHLVEAL + H2O = FVNQHLCGSHLVE + L-Ala-L-Leu + L-Leu

0

-

3.4.21.25

Leu-Leu-Leu-Leu-Pro-Glu-Ala-Leu + H2O = Leu-Leu-Leu-Leu-Pro-Glu + Ala-Leu

650612

-

3.4.21.25

Leu-Leu-Leu-Pro-Glu-Ala-Leu + H2O = Leu-Leu-Leu-Pro-Glu + Ala-Leu

650612

-

3.4.21.25

Leu-Leu-Pro-Ala-Ala-Leu + H2O = Leu-Leu-Pro-Ala + Ala-Leu

650612

-

3.4.21.25

Leu-Leu-Pro-Arg-Ala-Leu + H2O = Leu-Leu-Pro-Arg + Ala-Leu

650612

-

3.4.21.25

Leu-Leu-Pro-Asn-Ala-Leu + H2O = Leu-Leu-Pro-Asn + Ala-Leu

650612

-

3.4.21.25

Leu-Leu-Pro-Asp-Ala-Leu + H2O = Leu-Leu-Pro-Asp + Ala-Leu

650612

-

3.4.21.25

Leu-Leu-Pro-Gln-Ala-Leu + H2O = Leu-Leu-Pro-Gln + Ala-Leu

650612

-

3.4.21.25

Leu-Leu-Pro-Glu-Ala-Leu + H2O = Leu-Leu-Pro-Glu + Ala-Leu

650612

-

3.4.21.25

Leu-Leu-Pro-His-Ala-Leu + H2O = Leu-Leu-Pro-His + Ala-Leu

650612

-

3.4.21.25

Leu-Leu-Pro-Leu-Ala-Leu + H2O = Leu-Leu-Pro-Leu + Ala-Leu

650612

-

3.4.21.25

Leu-Leu-Pro-Lys-Ala-Leu + H2O = Leu-Leu-Pro-Lys + Ala-Leu

650612

-

3.4.21.25

Leu-Leu-Pro-Met-Ala-Leu + H2O = Leu-Leu-Pro-Met + Ala-Leu

0, 650612

-

3.4.21.25

Leu-Leu-Pro-Phe-Ala-Leu + H2O = Leu-Leu-Pro-Phe + Ala-Leu

650612

-

3.4.21.25

Leu-Leu-Pro-Ser-Ala-Leu + H2O = Leu-Leu-Pro-Ser + Ala-Leu

650612

-

3.4.21.25

Leu-Leu-Pro-Thr-Ala-Leu + H2O = Leu-Leu-Pro-Thr + Ala-Leu

650612

-

3.4.21.25

Leu-Leu-Pro-Trp-Ala-Leu + H2O = Leu-Leu-Pro-Trp + Ala-Leu

650612

-

3.4.21.25

Leu-Pro-Glu-Ala-Leu + H2O = Leu-Pro-Glu + Ala-Leu

650612

-

3.4.21.25

17 entries

3.4.21.42

GLQRAL + H2O = GLQR + Ala-Leu

650199

-

3.4.23.12

FVNQHLCGSHLVEALYLVCGERGFFYTPKA + H2O = FVNQHL + CGSHLVE + Ala-Leu + Tyr + LVCGERGF + FYTPKA

0

-

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

3.4.13.18

1190

-

phosphate buffer

137184

3.4.13.18

6510

-

Tris buffer

137184

3.4.13.18

2 entries

K_M Value (4 results)

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Show KM Value (4 entries)

EC NUMBER

KM VALUE [MM]

KM VALUE MAXIMUM [MM]

COMMENTARY

LITERATURE

3.4.13.18

0.28

-

tumor enzyme

137178

3.4.13.18

0.4

-

-

137179

3.4.13.18

0.44

-

Tris buffer

137184

3.4.13.18

1

-

phosphate buffer

137184

3.4.13.18

4 entries

References & Links

Literature References (19)

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Show Reference (19 entries)

BRENDA REFERENCE ID

PUBMED ID

TITLE

YEAR

AUTHORS

JOURNAL

VOLUME

PAGES

28298

5147

Yeast aminopeptidase I. Chemical composition and catalytic properties

1976

Metz, G.; Röhm.K.H.

Biochim. Biophys. Acta

429

933-949

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

36096

4280316

Partial purification and characterization of two peptidases from Neurospora crassa

1974

Johnson, G.L.; Brown, J.L.

Biochim. Biophys. Acta

370

530-540

95731

9223006

The Application of papain, ficin and clostripain in kinetically controlled peptide synthesis in frozen aqueous solutions

1995

Hänsler, M.; Ullmann, G.; Jakubke, H.D.

J. Pept. Sci.

1

283-287

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

137178

4596146

Substrate specificity and pH dependence of dipeptidases purified from Escherichia coli B and from mouse ascites tumor cells

1973

Patterson, E.K.; Gatmaitan, J.S.; Hayman, S.

Biochemistry

12

3701-3709

137179

5542681

Purification and properties of a mouse ascites tumor dipeptidase, a metalloenzyme

1971

Hayman, S.; Patterson, E.K.

J. Biol. Chem.

246

660-669

137184

4204951

Glycyl-L-leucine hydrolase, a versatile master dipeptidase from monkey small intestine

1973

Das, M.; Radhakrishnan, A.N.

Biochem. J.

135

609-615

137189

4628531

Substrate specificity of a highly active dipeptidase purified from monkey small intestine

1972

Das, M.; Radhakrishnan, A.N.

Biochem. J.

128

463-465

643878

10852868

Salmonella enterica serovar Typhimurium peptidase B is a leucyl aminopeptidase with specificity for acidic amino acids

2000

Mathew, Z.; Knox, T.M.; Miller, C.G.

J. Bacteriol.

182

3383-3393

647031

1012014

Human liver aminopeptidase

1976

Little, G.H.; Starnes, W.L.; Behal, F.J.

Methods Enzymol.

45

495-503

647116

1903095

Purification and properties of human serum carnosinase

1991

Jackson, M.C.; Kucera, C.M.; Lenney, J.F.

Clin. Chim. Acta

196

193-206

650199

14674770

Importance of the prime subsites of the C1s protease of the classical complement pathway for recognition of substrates

2003

O'Brien, G.; Quinsey, N.S.; Whisstock, J.C.; Pike, R.N.

Biochemistry

42

14939-14945

650612

11129582

Substrate specificity of cucumisin on synthetic peptides

2000

Yonezawa, H.; Kaizuka, H.; Uchikoba, T.; Arima, K.; Kaneda, M.

Biosci. Biotechnol. Biochem.

64

2104-2108

651057

10672029

Specificity of the wound-induced leucine aminopeptidase (LAP-A) of tomato. Activity on dipeptide and tripeptide substrates

2000

Gu, Y.Q.; Walling, L.L.

Eur. J. Biochem.

267

1178-1187

651119

11895433

Identification of residues critical for activity of the wound-induced leucine aminopeptidase (LAP-A) of tomato

2002

Gu, Y.Q.; Walling, L.L.

Eur. J. Biochem.

269

1630-1640

668856

-

Mucrolysin

2004

Komori, Y.; Nikai, T.

Handbook Of Proteolytic Enzymes(Barrett,A. J. ,Rawlings,N. D. ,Woessner,J. F. ,Eds. )Academic Press

1

705-706

677698

17601807

Characterization of a Bifidobacterium longum BORI dipeptidase belonging to the U34 family

2007

Seo, J.M.; Ji, G.E.; Cho, S.H.; Park, M.S.; Lee, H.J.

Appl. Environ. Microbiol.

73

5598-5606

729191

11747447

Evolution of enzymatic activities in the enolase superfamily: functional assignment of unknown proteins in Bacillus subtilis and Escherichia coli as L-Ala-D/L-Glu epimerases

2001

Schmidt, D.M.; Hubbard, B.K.; Gerlt, J.A.

Biochemistry

40

15707-15715

Links to other databases for Ala-Leu

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Show Links (1 entry)

ChEBI

PubChem