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Literature summary for 4.3.2.5 extracted from

  • Moore, A.B.; May, S.W.
    Kinetic and inhibition studies on substrate channelling in the bifunctional enzyme catalysing C-terminal amidation (1999), Biochem. J., 341, 33-40.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 4.3.2.5

Cloned(Commentary)

Cloned (Comment) Organism
expression in cultured Sf9 insect cells Xenopus laevis

Inhibitors

Inhibitors Comment Organism Structure
acetylmethionyl pyruvate competitive inhibition of PGL domain of full expressed enzyme: AE and monofunctional lyase: PGL Xenopus laevis
acetylphenylalanyl pyruvate competitive inhibition of PGL domain of full expressed enzyme: AE and monofunctional lyase: PGL Xenopus laevis
acetyltyrosyl pyruvate competitive inhibition of PGL domain of full expressed enzyme: AE and monofunctional lyase: PGL Xenopus laevis
additional information
-
 Bos taurus
additional information the inhibitors of PAM: acetyl-L-Phe-acetic acid and [(4-methoxybenzoyl)oxy]acetic acid show no effect of the KM of the monofunctional lyase: PGL Xenopus laevis

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.014
-
 trinitrophenyl-D-Tyr-L-Val-alpha-hydroxy-Gly 37°C, pH 6.6, PGL domain of transmembrane truncated enzyme: dAE Xenopus laevis
0.018
-
 trinitrophenyl-D-Tyr-L-Val-alpha-hydroxy-Gly 37°C, pH 6.6, PGL domain of full expressed enzyme: AE Xenopus laevis
0.019
-
 trinitrophenyl-D-Tyr-L-Val-alpha-hydroxy-Gly 37°C, pH 6.6, monofunctional lyase: PGL Xenopus laevis
0.033
-
 trinitrophenyl-D-Tyr-L-Val-alpha-hydroxy-Gly 37°C, pH 6.6 Bos taurus

Organism

Organism UniProt Comment Textmining
Bos taurus
-
-
-
Xenopus laevis
-
-
-

Purification (Commentary)

Purification (Comment) Organism
-
 Xenopus laevis

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
23000
-
 PGL domain of full expressed enzyme: AE Xenopus laevis
76000
-
 PGL domain of transmembrane truncated enzyme: dAE Xenopus laevis
180000
-
 monofunctional lyase: PGL Xenopus laevis

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
trinitrophenyl-D-Tyr-L-Val-alpha-hydroxy-Gly
-
 Bos taurus trinitrophenyl-D-Tyr-L-Val-NH2 + glyoxylate
-
 ?
trinitrophenyl-D-Tyr-L-Val-alpha-hydroxy-Gly
-
 Xenopus laevis trinitrophenyl-D-Tyr-L-Val-NH2 + glyoxylate
-
 ?

Ki Value [mM]

Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
0.049
-
 acetylphenylalanyl pyruvate 37°C, pH 6.6, monofunctional lyase: PGL Xenopus laevis
0.071
-
 acetylphenylalanyl pyruvate 37°C, pH 6.6, PGL domain of full expressed enzyme: AE Xenopus laevis
0.55
-
 acetyltyrosyl pyruvate 37°C, pH 6.6, monofunctional lyase: PGL Xenopus laevis
0.92
-
 acetyltyrosyl pyruvate 37°C, pH 6.6, PGL domain of full expressed enzyme: AE Xenopus laevis
3.2
-
 acetylmethionyl pyruvate 37°C, pH 6.6, monofunctional lyase: PGL Xenopus laevis
4.8
-
 acetylmethionyl pyruvate 37°C, pH 6.6, PGL domain of full expressed enzyme: AE Xenopus laevis