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Literature summary for 3.4.23.1 extracted from

  • Miura, Y.; Suzuki-Matsubara, M.; Kageyama, T.; Moriyama, A.
    Structure, molecular evolution, and hydrolytic specificities of largemouth bass pepsins (2016), Comp. Biochem. Physiol. B, 192, 49-59 .
    View publication on PubMed
Search for more literature for 3.4.23.1

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.04
-
 KPAEFFRL at pH 4.0 and 30°C Sus scrofa
0.05
-
 KPAEFFRL pepsin A1, at pH 4.0 and 30°C Micropterus salmoides
0.06
-
 KPAEFFRL at pH 4.0 and 37°C Sus scrofa
0.06
-
 KPAEFFRL at pH 4.0 and 45°C Sus scrofa
0.08
-
 KPAEFFRL pepsin A1, at pH 4.0 and 37°C Micropterus salmoides
0.1
-
 KPAEFFRL at pH 4.0 and 20°C Sus scrofa
0.1
-
 KPAEFFRL pepsin A2, at pH 4.0 and 10°C Micropterus salmoides
0.11
-
 KPAEFFRL pepsin A2, at pH 4.0 and 20°C Micropterus salmoides
0.12
-
 KPAEFFRL pepsin A2, at pH 4.0 and 30°C Micropterus salmoides
0.13
-
 KPAEFFRL pepsin A1, at pH 4.0 and 45°C Micropterus salmoides
0.14
-
 KPAEFFRL at pH 4.0 and 10°C Sus scrofa
0.14
-
 KPAEFFRL pepsin A2, at pH 4.0 and 37°C Micropterus salmoides
0.2
-
 KPAEFFRL pepsin A1, at pH 4.0 and 20°C Micropterus salmoides
0.24
-
 KPAEFFRL pepsin A2, at pH 4.0 and 45°C Micropterus salmoides
0.3
-
 KPAEFFRL pepsin A1, at pH 4.0 and 10°C Micropterus salmoides

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
additional information Micropterus salmoides the enzyme prefers both hydrophobic/aromatic residues and charged residues at the P'1 sites of substrates. Pepsin A1 does not prefer some hydrophobic residues such as Leu, Val, Ala and Met ?
-
 ?
additional information Micropterus salmoides the enzyme prefers both hydrophobic/aromatic residues and charged residues at the P'1 sites of substrates. Pepsin A2 does not prefer some hydrophobic residues such as Leu, Val, Ala and Met ?
-
 ?
additional information Sus scrofa the enzyme prefers both hydrophobic/aromatic residues and charged residues at the P'1 sites of substrates. The enzyme prefers some hydrophobic residues such as Leu, Val, Ala and Met ?
-
 ?

Organism

Organism UniProt Comment Textmining
Micropterus salmoides A0A125SQG8 largemouth bass
-
Micropterus salmoides A0A125SQG9 largemouth bass
-
Sus scrofa
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
KPAEFFRL + H2O
-
 Sus scrofa KPAEF + FRL
-
 ?
KPAEFFRL + H2O
-
 Micropterus salmoides KPAEF + FRL
-
 ?
KPAEFIRL + H2O
-
 Micropterus salmoides KPAEF + IRL
-
 ?
KPAEFIRL + H2O best substrate for pepsin A1 Micropterus salmoides KPAEF + IRL
-
 ?
KPAEFRRL + H2O
-
 Sus scrofa KPAEF + RRL
-
 ?
KPAEFRRL + H2O
-
 Micropterus salmoides KPAEF + RRL
-
 ?
KPAEFWRL + H2O
-
 Micropterus salmoides KPAEF + WRL
-
 ?
KPAEFWRL + H2O best substrate for pepsin A2 Micropterus salmoides KPAEF + WRL
-
 ?
KPAQFFRL + H2O best substrate Sus scrofa KPAQF + FRL
-
 ?
additional information the enzyme prefers both hydrophobic/aromatic residues and charged residues at the P'1 sites of substrates. Pepsin A1 does not prefer some hydrophobic residues such as Leu, Val, Ala and Met Micropterus salmoides ?
-
 ?
additional information the enzyme prefers both hydrophobic/aromatic residues and charged residues at the P'1 sites of substrates. Pepsin A2 does not prefer some hydrophobic residues such as Leu, Val, Ala and Met Micropterus salmoides ?
-
 ?
additional information the enzyme prefers both hydrophobic/aromatic residues and charged residues at the P'1 sites of substrates. The enzyme prefers some hydrophobic residues such as Leu, Val, Ala and Met Sus scrofa ?
-
 ?

Synonyms

Synonyms Comment Organism
pepsin A1
-
 Micropterus salmoides
pepsin A2
-
 Micropterus salmoides
PG1
-
 Micropterus salmoides
PG2
-
 Micropterus salmoides

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
4.69
-
 KPAEFFRL pepsin A1, at pH 4.0 and 10°C Micropterus salmoides
4.92
-
 KPAEFFRL pepsin A1, at pH 4.0 and 20°C Micropterus salmoides
8.19
-
 KPAEFFRL pepsin A1, at pH 4.0 and 30°C Micropterus salmoides
9.73
-
 KPAEFFRL at pH 4.0 and 10°C Sus scrofa
12.4
-
 KPAEFFRL at pH 4.0 and 20°C Sus scrofa
18.6
-
 KPAEFFRL pepsin A1, at pH 4.0 and 37°C Micropterus salmoides
18.7
-
 KPAEFFRL pepsin A2, at pH 4.0 and 10°C Micropterus salmoides
21.9
-
 KPAEFFRL at pH 4.0 and 30°C Sus scrofa
28.9
-
 KPAEFFRL pepsin A2, at pH 4.0 and 20°C Micropterus salmoides
33.3
-
 KPAEFFRL at pH 4.0 and 37°C Sus scrofa
36.5
-
 KPAEFFRL pepsin A1, at pH 4.0 and 45°C Micropterus salmoides
74.7
-
 KPAEFFRL pepsin A2, at pH 4.0 and 30°C Micropterus salmoides
75.9
-
 KPAEFFRL at pH 4.0 and 45°C Sus scrofa
139.2
-
 KPAEFFRL pepsin A2, at pH 4.0 and 37°C Micropterus salmoides
215.5
-
 KPAEFFRL pepsin A2, at pH 4.0 and 45°C Micropterus salmoides

kcat/KM [mM/s]

kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
19.9
-
 KPAEFFRL pepsin A1, at pH 4.0 and 10°C Micropterus salmoides
36.8
-
 KPAEFFRL pepsin A1, at pH 4.0 and 20°C Micropterus salmoides
70.2
-
 KPAEFFRL at pH 4.0 and 10°C Sus scrofa
164.6
-
 KPAEFFRL pepsin A1, at pH 4.0 and 30°C Micropterus salmoides
186.2
-
 KPAEFFRL at pH 4.0 and 20°C Sus scrofa
218.5
-
 KPAEFFRL pepsin A2, at pH 4.0 and 10°C Micropterus salmoides
251.3
-
 KPAEFFRL pepsin A1, at pH 4.0 and 37°C Micropterus salmoides
283
-
 KPAEFFRL pepsin A2, at pH 4.0 and 20°C Micropterus salmoides
286.3
-
 KPAEFFRL pepsin A1, at pH 4.0 and 45°C Micropterus salmoides
475.4
-
 KPAEFFRL at pH 4.0 and 30°C Sus scrofa
598.9
-
 KPAEFFRL at pH 4.0 and 37°C Sus scrofa
604.8
-
 KPAEFFRL pepsin A2, at pH 4.0 and 30°C Micropterus salmoides
959.9
-
 KPAEFFRL pepsin A2, at pH 4.0 and 45°C Micropterus salmoides
999.6
-
 KPAEFFRL pepsin A2, at pH 4.0 and 37°C Micropterus salmoides
1306.2
-
 KPAEFFRL at pH 4.0 and 45°C Sus scrofa