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Literature summary for 1.6.5.5 extracted from

  • Kim, S.; Mori, T.; Chek, M.; Furuya, S.; Matsumoto, K.; Yajima, T.; Ogura, T.; Hakoshima, T.
    Structural insights into vesicle amine transport-1 (VAT-1) as a member of the NADPH-dependent quinone oxidoreductase family (2021), Sci. Rep., 11, 2120 .
    View publication on PubMedView publication on EuropePMC

Crystallization (Commentary)

Crystallization (Comment) Organism
structure in the free state at 2.3 A resolution. VAT-1 forms a dimer with the conserved NADPH-binding cleft on each protomer. The structure of VAT-1 in the NADP-bound state at 2.6 A resolution shows that NADP binds the binding cleft to create a putative active site with the nicotine ring Homo sapiens

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.0299
-
9,10-phenanthrenequinone pH 7.8, 25°C Homo sapiens

Localization

Localization Comment Organism GeneOntology No. Textmining
mitochondrion
-
Homo sapiens 5739
-

Organism

Organism UniProt Comment Textmining
Homo sapiens A0A024R1Z6
-
-

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
0.64
-
substrate 9,10-phenanthrenequinone, pH 7.8, 25°C Homo sapiens

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1,2-naphthoquinone + NADPH + H+
-
Homo sapiens 1,2-naphthoquinol + NADP+
-
?
9,10-phenanthrenequinone + NADPH + H+
-
Homo sapiens 9,10-phenanthrenequinol + NADP+
-
?

Synonyms

Synonyms Comment Organism
VAT-1
-
Homo sapiens
vesicle amine transport protein-1
-
Homo sapiens

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
1.13
-
9,10-phenanthrenequinone pH 7.8, 25°C Homo sapiens

kcat/KM [mM/s]

kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
37.8
-
9,10-phenanthrenequinone pH 7.8, 25°C Homo sapiens