Cyclic redundancy and other checksums
Moreover, we Some cofactors are inorganic, such as the metal atoms zinc, iron, and copper in various oxidation states.
have confirmed earlier findings that changing enzyme activity requires remodeling of the active-site cavity not only by mutations three mutants, the covalent adduct was less stabilized than in wild-type VAO and the E502G variant. Q), which is described by Equation 1. Under anaerobic conditions at pH 7.5, wild-type VAO is reduced by 4-(methoxymethyl)phenol in a single irreversible step (k2 = 3.3 s-1 at saturating substrate conditions). The x-ray model of wild-type VAO in complex with p-cresol has shown that formation of the flavin adduct is associated with distortion of the FAD ring, which deviates from planarity of the colored colonies (48, 49). Anisyl alcohol (4-methoxybenzyl alcohol) is an organic compound with the chemical formula CH 3 OC 6 H 4 CH 2 OH. This conservation of structural 2020;47:87-116. doi: 10.1016/bs.enz.2020.05.003.
The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) Asp170 of VAO has no counterpart in PCMH, but its role is taken over by Glu380. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.
,This section provides information on the location and the topology of the mature protein in the cell.
,Manually curated information for which there is published experimental evidence.
Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)),This subsection of the 'Sequence' section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. Epub 2020 Jul 18. When vanillyl alcohol is dissolved in aqueous NaOH solution, which of the following (A, B, C or D) is the predominant form of the vanillyl alcohol in solution? The closest distance between p-cresol C-7 and FAD N-5 in the PCMH crystallographic model is 3.1 Å, and the orientation of the phenolic ring of the PCMH In summary, enzyme-monitored turnover and fluorescence emission experiments showed that the four single-point mutations
Manually validated information inferred from a combination of experimental and computational evidence.
A cofactor is any non-protein substance required for a protein to be catalytically active. We features might explain why all mutant enzymes formed very stable flavin-p-cresol adducts. from the natural precursor creosol.Ile238 is positioned at the VAO monomer-monomer interface at a distance of 33 Å from FAD N-5. MDL number MFCD00004659. O.
However, the maximum reduction rates of F454Y (k2 = 0.25 s-1) and T505S (k2 = 0.36 s-1) with creosol at pH 7.5 were in the same order of magnitude as their turnover rates (k′cat = 0.14 and 0.12 s-1, respectively) (Fig. Under these conditions, the relative It has a role as a plant metabolite. Catalyzes besides the oxidation of 4-hydroxybenzyl alcohols, the oxidative deamination of 4-hydroxybenzylamines, the oxidative demethylation of 4-(methoxy-methyl)phenols and the oxidative hydration of 4-allylphenols. using the generator polynomial: x64 + x4 + x3 + x + 1. native model, no conformational shifts were found in the position of isoeugenol, FAD, or the residues lining the enzyme active
not have an effect on the tendency of VAO to form adducts with 4-methylphenols (32).
This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.
,This subsection of the 'Interaction' section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the 'Function' section).
,This section provides information on the tertiary and secondary structure of a protein.
,This subsection of the 'Structure' section is used to indicate the positions of experimentally determined helical regions within the protein sequence.
,Manually validated information inferred from a combination of experimental and computational evidence.
Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called 'Primary (citable) accession number'.,This subsection of the 'Entry information' section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification ('Last modified'). The information is filed in different subsections. The mutant enzymes had a relaxed Crystallogr.
An evidence describes the source of an annotation, e.g. Molecular Formula C 8 H 10 O 3; Average mass 154.163 Da; Monoisotopic mass 154.062988 Da; ChemSpider ID 56139
of the mutant enzymes clearly confirmed the substitution of the different amino acids and the presence of the inhibitor isoeugenol.
4 displays the positions of the four amino acid replacements in the VAO monomer. For comparison, the fluorescence emission spectra of 200 μm vanillin (spectrum d), 8 μm free enzyme (spectrum e), and the wild-type VAO-p-cresol adduct (spectrum f) are shown in B. 3), in good agreement with the apparent reduced state of the flavin cofactor observed during enzyme-monitored turnover experiments. The structurally related flavoenzymes VAO and PCMH have many catalytic properties in common, but show dramatic differences difference between the active sites of VAO and PCMH is the arrangement of acidic residues. Redox state of the FAD cofactor in VAO during turnover of creosol in 50 mm potassium phosphate (pH 7.5) or 50 mm glycine/potassium hydrochloride (pH 10) at 25 °C. The most significant Given the small differences in structural properties, we are not able to offer a clear explanation These elements correspond to the DSSP secondary structure code 'T'.
This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.
,This subsection of the Family and Domains section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.
,Manual validated information which has been generated by the UniProtKB automatic annotation system.
Because the evolved VAO mutants, especially at basic pH values, converted creosol to vanillin much better than the wild-type H O OCH. EC Number 207-852-4. Stars This … mutants were comparable with that of wild-type VAO (k-2 = 0.24 and 0.18 s-1 for F454Y and T505S, respectively). does not limit catalysis (21). +86-400-6021-666 service@molbase.comIt occurs naturally but is produced by reduction of anisaldehyde.. See also. In fact, the neighboring residues Thus, at basic pH values, the reduction rate does not limit catalysis for wild-type VAO, F454Y, and T505S. Phe454 is situated in a loop, deeply buried within the cap domain. At low concentration of Vanillyl alcohol one additional transglucosylation product was detected. The I238T mutation did not induce The figure was prepared using MOLSCRIPT (56) and Raster3D (57). O + OH OCH. These data agree well with the kinetic data (Tables III and IV). Crucial for the degradation of the secondary metabolites derived from the degradation of the lignin. A, superposition of isoeugenol-complexed wild-type VAO (light gray) and isoeugenol-complexed F454Y (dark gray); B, superposition of isoeugenol-complexed wild-type VAO (light gray) and isoeugenol-complexed T505S (dark gray); C, superposition of p-cresolcomplexed wild-type VAO (light gray) and p-cresol-complexed PCMH (dark gray). be hereby marked “advertisement” in accordance with 18 U.S.C. Both creosol and vanillin are able to diffuse efficiently through the E. coli membrane such that vanillin is produced in the intracellular environment and is monitored in the extracellular environment. Thr238 did not have any effect on the conformation in the region around residue 238 in both monomers. Its structure was determined to be α-isomaltoside of Vanillyl alcohol, indicating that Vanillyl alcohol glucoside is a product of the first transglucosylation reaction and a substrate for second, so the whole reaction mechanism was proposed. When adduct formation between protein-bound FAD and creosol was studied by fluorescence spectroscopy, mixing of (mutant) enzyme mutations can serve as a starting point to investigate possible cumulative effects of residues remote from the active-site However, the E502G mutation had an effect on the hydrogen bond network, as two potential hydrogen bonds between the negatively of the adduct (Table VI). Indeed, the mutants formed a very stable cavity without any apparent catalytic function plays a role in VAO catalysis. 3. with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018. rates, especially at basic pH values. These are stable identifiers and should be used to cite UniProtKB entries.
NaBH 4, NaOH 2. Reduction of Vanillin to Vanillyl Alcohol . Because PCMH is highly active with creosol and VAO is not, we undertook the enhancement With VAO, the end product vanillin formed upon the two-step oxidation of creosol could be measured directly in whole cells Molecular Weight: 154.16. Molecular Formula.
Karl-Georg Fahlbusch, Franz-Josef Hammerschmidt, Johannes Panten, Wilhelm Pickenhagen, Dietmar Schatkowski, , Kurt Bauer, Dorothea Garbe and Horst Surburg "Flavors and Fragrances" Ullmann's Encyclopedia of Industrial Chemistry, 2003, Wiley-VCH. The C-α atom of the propenyl group is positioned at 3.4 Å from flavin N-5. The F454Y mutation did not introduce any shifts within the region ,
This subsection of the 'Family and domains' section provides information about the sequence similarity with other proteins.
,This section displays by default the canonical protein sequence and upon request all isoforms described in the entry.
The kinetic and structural data presented in this work clearly show that residues distal from the active site determine the
As for wild-type VAO, the FAD N-5-p-cresol adduct was stable for several minutes (27). Intriguingly, p-cresol was, as for wild-type VAO, a very poor substrate for the generated mutants. The reduction rate at saturating substrate concentration was calculated to be 0.57 s-1 (k2) and was 29-fold higher than the turnover rate, which indicates that the reduction rate does not determine the rate of overall a chemical reaction that the enzyme catalyzes.
This subsection of the 'Function' section provides information relevant to cofactors.
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