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Literature summary for 1.5.1.36 extracted from

  • Yuenyao, A.; Petchyam, N.; Kamonsutthipaijit, N.; Chaiyen, P.; Pakotiprapha, D.
    Crystal structure of the flavin reductase of Acinetobacter baumannii p-hydroxyphenylacetate 3-hydroxylase (HPAH) and identification of amino acid residues underlying its regulation by aromatic ligands (2018), Arch. Biochem. Biophys., 653, 24-38 .
    View publication on PubMed
Search for more literature for 1.5.1.36

Activating Compound

Activating Compound Comment Organism Structure
4-hydroxyphenylacetic acid C1-HpaH undergoes a substantial conformational change in the presence of 4-hydroxyphenylacetic acid, concomitant with the increase in the rate of flavin reduction Acinetobacter baumannii

Crystallization (Commentary)

Crystallization (Comment) Organism
P3121 space group, to 2.9 A resolution. Each protomer of C1 contains one molecule of FMN in the nucleotide binding pocket. C1-HpaH undergoes a substantial conformational change in the presence of 4-hydroxyphenylacetic acid, concomitant with the increase in the rate of flavin reduction Acinetobacter baumannii

Protein Variants

Protein Variants Comment Organism
E248A residue of the of the recognition helix of the MarR domain, activation by 4-hydroxyphenylacetic acid similarly to wild-type, high constitutive NADH oxidation activity without auto-inhibition Acinetobacter baumannii
E251A residue of the of the recognition helix of the MarR domain, activation by 4-hydroxyphenylacetic acid similarly to wild-type, high constitutive NADH oxidation activity without auto-inhibition Acinetobacter baumannii
F216A high constitutive NADH oxidation activity without auto-inhibition Acinetobacter baumannii
H170A putative residue of the 4-hydroxyphenylacetic acid binding site, activation by 4-hydroxyphenylacetic acid similarly to wild-type Acinetobacter baumannii
N174A putative residue of the 4-hydroxyphenylacetic acid binding site, activation by 4-hydroxyphenylacetic acid similarly to wild-type Acinetobacter baumannii
R20A residue of flavin reductase domain, activation by 4-hydroxyphenylacetic acid similarly to wild-type Acinetobacter baumannii
S172A putative residue of the 4-hydroxyphenylacetic acid binding site, activation by 4-hydroxyphenylacetic acid similarly to wild-type Acinetobacter baumannii
Y207A putative residue of the 4-hydroxyphenylacetic acid binding site, no activation by 4-hydroxyphenylacetic acid along with low NADH oxidation rate Acinetobacter baumannii

Inhibitors

Inhibitors Comment Organism Structure
MarR auto-inhibition by the C-terminal MarR domain, which might arise from steric hindrance Acinetobacter baumannii

Organism

Organism UniProt Comment Textmining
Acinetobacter baumannii Q6Q271
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-

Synonyms

Synonyms Comment Organism
C1-HpaH
-
 Acinetobacter baumannii