| Title | Enzymatic carboxylation of hydroxystilbenes by the γ-resorcylic acid decarboxylase from Rhizobium radiobacter WU-0108 under reverse reaction conditions |
|---|---|
| Author | Masaru Sato, Nozomu Sakurai, Hideyuki Suzuki, Daisuke Shibata, Kuniki Kino |
| DOI | 10.1016/j.molcatb.2015.10.006 |
| Abstract | We examined 66 aromatics for carboxylation by the γ-resorcylic acid decarboxylase from Rhizobium radiobacter WU-0108 under reverse reaction conditions. The enzyme carboxylated resorcinol, catechol, 5-methylresorcinol and three hydroxystilbenes (resveratrol, gnetol, and piceatannol) with high yields. Except for catechol, the structures of these substrates include a 1,3-dihydroxybenzene moiety. Other compounds gave no reaction products. The reaction products from resveratrol and gnetol were 2,6-dihydroxy-4-[(E)-2-(4-hydroxyphenyl)ethenyl]benzoic acid and 2,6-dihydroxy-4-[(E)-2-(2,6-dihydroxyphenyl)ethenyl] benzoic acid, respectively, as determined by mass spectrometry and nuclear magnetic resonance analyses. Kinetic analyses of the carboxylation reactions indicated that resveratrol and gnetol are better substrates than resorcinol or catechol. |
Uniprot ID: Q60FX6
Protein: Reversible 2,6-dihydroxybenzoic acid decarboxylase
Organism: Rhizobium radiobacter (Agrobacterium tumefaciens) (Agrobacterium radiobacter)
Length: 327 AA
Taxonomic identifier: 358 [NCBI]
| Source | Domain | Start | End | E-value (Domain) | Coverage |
|---|---|---|---|---|---|
| Pfam-A | Amidohydro_2 | 35 | 324 | 3.3e-47 | 0.931 |
Program: hmmscan
Version: 3.1b2 (February 2015)
Method: hmmscan --domtblout hmmscan.tbl --noali -E 1e-5 pfam query.fa
Date: Mon Jul 20 14:32:16 2020
Description:
Amidohydro_2
These proteins are amidohydrolases that are related to PF019791.
Proteins containing this domain are enzymes from a large metal dependent hydrolase superfamily1. The family includes adenine deaminase (3.5.4.2) that hydrolyses adenine to form hypoxanthine and ammonia. This reaction is important for adenine utilisation as a purine and also as a nitrogen source2. The family also includes dihydroorotase and N-acetylglucosamine-6-phosphate deacetylases (3.5.1.25). The domain is also found in the urease alpha subunit, where it is the catalytic domain3.
Information is taken from Pfam and InterPro web site.
resveratrol ⇒ 2,6-Dihydroxy-4-[(E)-2-(4-hydroxyphenyl)ethenyl]benzoic acid
![[L1]resveratrol](../static/images/chemical_structure/NCR1/[L1]resveratrol.png)
![[R1]2,6-Dihydroxy-4-[(E)-2-(4-hydroxyphenyl)ethenyl]benzoic acid.png](../static/images/chemical_structure/NCR1/[R1]2,6-Dihydroxy-4-[(E)-2-(4-hydroxyphenyl)ethenyl]benzoic acid.png)
Holm L, Sander C. An evolutionary treasure: unification of a broad set of amidohydrolases related to urease[J]. Proteins: Structure, Function, and Bioinformatics, 1997, 28(1): 72-82. ↩↩
Nygaard P, Duckert P, Saxild H H. Role of adenine deaminase in purine salvage and nitrogen metabolism and characterization of the ade gene in Bacillus subtilis[J]. Journal of Bacteriology, 1996, 178(3): 846-853. ↩
Jabri E, Carr M B, Hausinger R P, et al. The crystal structure of urease from Klebsiella aerogenes[J]. Science, 1995, 268(5213): 998-1004. ↩