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Ligand L-Gln-L-Phe-L-Ala-NH2

Basic Ligand Information

Molecular Structure

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Roles as Enzyme Ligand

Substrate in Enzyme-catalyzed Reactions (4 results)

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Show Substrate (4 entries)

EC NUMBER

REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

2.3.2.5

Gln-Phe-Ala-NH2 = pyroglutamic acid-Phe-Ala-NH2 + NH3

658233

-

2.3.2.5

H-Gln-Phe-Ala-NH2 = 5-oxoprolyl-Phe-Ala-NH2 + NH3

672479

-

2.3.2.5

L-Gln-L-Phe-L-Ala-NH2 = 5-oxoprolyl-L-Phe-L-Ala-NH2 + NH3

718904, 719267

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2.3.2.5

L-Gln-L-Phe-L-Ala-NH2 = L-pyroglutamyl-L-Phe-L-Ala-NH2 + NH3

672479

-

2.3.2.5

4 entries

Enzyme Kinetic Parameters

k_cat Value (Turnover Number) (6 results)

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Show Turnover Number (6 entries)

EC NUMBER

TURNOVER NUMBER [1/S]

TURNOVER NUMBER MAXIMUM [1/S]

COMMENTARY

LITERATURE

2.3.2.5

55

-

pH 8.0, 30°C

672479

2.3.2.5

55

-

pH 8.0, 30°C

672479

2.3.2.5

57

-

pH 8.0, 30°C

672479

2.3.2.5

57

-

pH 8.0, 30°C

672479

2.3.2.5

109

-

pH 8.0, 30°C

658233

2.3.2.5

132

-

pH 8.0, 30°C

658233

2.3.2.5

6 entries

K_M Value (6 results)

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Show KM Value (6 entries)

EC NUMBER

KM VALUE [MM]

KM VALUE MAXIMUM [MM]

COMMENTARY

LITERATURE

2.3.2.5

0.069

-

pH 8.0, 30°C

658233

2.3.2.5

0.106

-

pH 8.0, 30°C

672479

2.3.2.5

0.106

-

pH 8.0, 30°C

672479

2.3.2.5

0.111

-

pH 8.0, 30°C

658233

2.3.2.5

0.44

-

pH 8.0, 30°C

672479

2.3.2.5

0.44

-

pH 8.0, 30°C

672479

2.3.2.5

6 entries

References & Links

Literature References (4)

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Show Reference (4 entries)

BRENDA REFERENCE ID

PUBMED ID

TITLE

YEAR

AUTHORS

JOURNAL

VOLUME

PAGES

658233

14719800

Substrate specificity of glutaminyl cyclases from plants and animals

2003

Schilling, S.; Manhart, S.; Hoffmann, T.; Ludwig, H.H.; Wasternack, C.; Demuth, H.U.

Biol. Chem.

384

1583-1592

672479

17261077

Isolation and characterization of the glutaminyl cyclases from Solanum tuberosum and Arabidopsis thaliana: implications for physiological functions

2007

Schilling, S.; Stenzel, I.; von Bohlen, A.; Wermann, M.; Schulz, K.; Demuth, H.U.; Wasternack, C.

Biol. Chem.

388

145-153

718904

21671571

Structures of glycosylated mammalian glutaminyl cyclases reveal conformational variability near the active center

2011

Ruiz-Carrillo, D.; Koch, B.; Parthier, C.; Wermann, M.; Dambe, T.; Buchholz, M.; Ludwig, H.H.; Heiser, U.; Rahfeld, J.U.; Stubbs, M.T.; Schilling, S.; Demuth, H.U.

Biochemistry

50

6280-6288

719267

22967026

Probing secondary glutaminyl cyclase (QC) inhibitor interactions applying an in silico-modeling/site-directed mutagenesis approach: implications for drug development

2012

Koch, B.; Buchholz, M.; Wermann, M.; Heiser, U.; Schilling, S.; Demuth, H.U.

Chem. Biol. Drug Des.

80

937-946

Links to other databases for L-Gln-L-Phe-L-Ala-NH2

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Show Links (1 entry)

ChEBI

PubChem

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