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Literature summary for 2.3.1.118 extracted from

  • Huang, K.; Gao, F.; Le, X.C.; Zhao, F.J.
    N-Hydroxyarylamine O-acetyltransferases catalyze acetylation of 3-amino-4-hydroxyphenylarsonic acid in the 4-hydroxy-3-nitrobenzenearsonic acid transformation pathway of Enterobacter sp. strain CZ-1 (2020), Appl. Environ. Microbiol., 86, e02050 .
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

Cloned (Comment) Organism
expression in Escherichia coli Enterobacter sp. CZ-1

Protein Variants

Protein Variants Comment Organism
C69A mutation in isoform NhoA1, inactive Enterobacter sp. CZ-1
C72A mutation in isoform NhoA2, inactive Enterobacter sp. CZ-1
R65A mutation if isoform NhoA1, inactive Enterobacter sp. CZ-1
R68A mutation in isoform NhoA2, inactive Enterobacter sp. CZ-1

Inhibitors

Inhibitors Comment Organism Structure
Al3+ moderate inhibition of isoform NhoA1 Enterobacter sp. CZ-1
Cr3+ moderate inhibition of isoform NhoA1 Enterobacter sp. CZ-1
Fe3+ 1 mM, complete inhibition of isoform NhoA1 Enterobacter sp. CZ-1
N-ethylmaleimide 1 mM, 65% inhibition of isoform NhoA1, 45% inhibition of isoform NhoA2 Enterobacter sp. CZ-1
paraoxon 0.1 mM, 23.5% inhibition of isoform NhoA1, 14% inhibition of isoform NhoA2 Enterobacter sp. CZ-1
Zn2+ moderate inhibition of both isoforms NhoA1 and NhoA2 Enterobacter sp. CZ-1

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.151
-
3-amino-4-hydroxyphenylarsonic acid isoform NhoA1, pH 7.4, 30°C Enterobacter sp. CZ-1
0.428
-
3-amino-4-hydroxyphenylarsonic acid isoform NhoA2, pH 7.4, 30°C Enterobacter sp. CZ-1

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
52500
-
gel filtration, isoform NhoA2 Enterobacter sp. CZ-1
66000
-
gel filtration, isoform NhoA1 Enterobacter sp. CZ-1

Organism

Organism UniProt Comment Textmining
Enterobacter sp. CZ-1
-
-
-

Storage Stability

Storage Stability Organism
4°C, elution buffer, 1 month, 89% residual activity for isoform NhoA1, 95% residual activity for isoform NhoA2, respectively Enterobacter sp. CZ-1

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
acetyl-CoA + 3-amino-4-hydroxyphenylarsonic acid
-
Enterobacter sp. CZ-1 CoA + N-acetyl-3-amino-4-hydroxyphenylarsonic acid
-
?
additional information no substrates of either isoform NhoA1 or NhoA2: 4-amino-phenylarsonic acid, 2-amino-phenylarsonic acid, and 4-carbamoylamino-phenylarsonic acid Enterobacter sp. CZ-1 ?
-
-

Subunits

Subunits Comment Organism
dimer 2 * 29600, SDS-PAGE, isoform NhoA2 Enterobacter sp. CZ-1
dimer 2 * 32700, SDS-PAGE, isoform NhoA1 Enterobacter sp. CZ-1

Synonyms

Synonyms Comment Organism
NhoA1
-
Enterobacter sp. CZ-1
NhoA2
-
Enterobacter sp. CZ-1

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
1.34
-
3-amino-4-hydroxyphenylarsonic acid isoform NhoA2, pH 7.4, 30°C Enterobacter sp. CZ-1
54.5
-
3-amino-4-hydroxyphenylarsonic acid isoform NhoA1, pH 7.4, 30°C Enterobacter sp. CZ-1

General Information

General Information Comment Organism
physiological function deletion of of isoforms NhoA1 and NhoA2 decreases 3-amino-4-hydroxyphenylarsonic acid acetylation activity by 97 and 14%, respectively, the double mutant loses the acetylation activity completely. Deletion of isoform NhoA1 increases the release of inorganic As(III) and As(V) from3 -amino-4-hydroxyphenylarsonic acid or roxarsone Enterobacter sp. CZ-1