Phenylalanine ammonia lyase from Rhodotorula glutinis

Enzyme Description

Species
Rhodotorula glutinis β†—
Extremophile
No
EC Number
4.3.1.5 β†—

Sequence

Length: 706 amino acids
MAPSVDSIATSVANSLSNGLAGDVRKKTSGAGSLLPTTETTQIDIVERILADAGATDQIKLDGYTLTLGDVVGAARHGRTVKVADSPQIREKIDASVEFLRTQLDNSVYGVTTGFGGSADTRTEDAISLQKALLEHQLCGVLPTSMDGFALGRGLENSLPLEVVRGAMTIRVNSLTRGHSAVRIVVLEALTNFLNHGITPIVPLRGTISASGDLSPLSYIAASITGHPDSKVHVDGKIMSAQEAIALKGLQPVVLGPKEGLGLVNGTAVSASMATLALTDAHVLSLLAQANTALTVEAMVGHAGSFHPFLHDVTRPHPTQIEVARNIRTLLEGSKYAVHHETEVKVKDDEGILRQDRYPLRCSPQWLGPLVSDMIHAHSVLSLEAGQSTTDNPLIDLENKMTHHGGAFMASSVGNTMEKTRLAVALMGKVSFTQLTEMLNAGMNRALPSCLAAEDPSLSYHCKGLDIAAAAYTSELGHLANPVSTHVQPAEMGNQAINSLALISARRTAEANDVLSLLLATHLYCVLQAVDLRAMEFEHTKEFEPMVTALLKQHLGALATADVEDKVRKSIYKRLQQNNSYDLEQRWHDTFSVATGAVVEALAGNEVSLASLNAWKVACAEKAIALTRTVRDSFWAAPSSSSPALKYLSPRTRILYSFIREDVGVKARRGDVYLGKQEVTIGTNVSRIYEAIKDGRIAPVLVKMMA
Andrew J. Quinn et al. (2011) β€” Enzyme activity evaluation of organic solvent-treated phenylalanine ammonia lyase
Biotechnology Progress  Β· doi:10.1002/btpr.687 β†—  Β· Stability - Incubation
40 measurements ▼
Database ID
UniProt: A0A3S5G0Z9 β†—
Sequence Annotation
Inferred - from protein name
Protein Source
Purified, yeast Rhodotorula glutinis

Experimental Data (40 measurements)

40 measurements β€” page 2 of 2
Property Assay Solvent Solvent Volume Aqueous Reference Measured Value Units Extraction method Data type Solution pH Temperature Substrate(s) Product(s) Cofactor(s) Shaking Comments
Stability - Incubation Activity after incubation (1 hour) of lyophilized enzyme, measured by absorbance spectrophotometry (Cinnamic acid absorbance measurement, 290 nm) in aqueous phase Methanol 100 % v/v 4.25 3.9 U Direct Continuous 100 mM Tris-HCl assay 8.8 30Β°C 37.5 mM L-Phenylalanine methyl ester Cinnamic acid methyl ester β€” Incubation: ultrasonication (50 Hz/s), Assay: 100 rpm Water-incubated control (in U) | Bit of uncertainty about protein sequence, lyophilized enzyme incubation
Stability - Incubation Activity after incubation (1 hour) of lyophilized enzyme, measured by absorbance spectrophotometry (Cinnamic acid absorbance measurement, 290 nm) in aqueous phase Ethanol 100 % v/v 4.7 4.4 U Direct Continuous 100 mM Tris-HCl assay 8.8 30Β°C 37.5 mM L-Phenylalanine Cinnamic acid β€” Incubation: ultrasonication (50 Hz/s), Assay: 100 rpm Water-incubated control (in U) | Bit of uncertainty about protein sequence, lyophilized enzyme incubation
Stability - Incubation Activity after incubation (1 hour) of lyophilized enzyme, measured by absorbance spectrophotometry (Cinnamic acid absorbance measurement, 290 nm) in aqueous phase Acetonitrile 100 % v/v 4.7 3.9 U Direct Continuous 100 mM Tris-HCl assay 8.8 30Β°C 37.5 mM L-Phenylalanine Cinnamic acid β€” Incubation: ultrasonication (50 Hz/s), Assay: 100 rpm Water-incubated control (in U) | Bit of uncertainty about protein sequence, lyophilized enzyme incubation
Stability - Incubation Activity after incubation (1 hour) of lyophilized enzyme, measured by absorbance spectrophotometry (Cinnamic acid absorbance measurement, 290 nm) in aqueous phase Acetone 100 % v/v 4.7 1.5 U Direct Continuous 100 mM Tris-HCl assay 8.8 30Β°C 37.5 mM L-Phenylalanine Cinnamic acid β€” Incubation: ultrasonication (50 Hz/s), Assay: 100 rpm Water-incubated control (in U) | Bit of uncertainty about protein sequence, lyophilized enzyme incubation
Stability - Incubation Activity after incubation (1 hour) of lyophilized enzyme, measured by absorbance spectrophotometry (Cinnamic acid absorbance measurement, 290 nm) in aqueous phase Dimethyl Sulfoxide (DMSO) 100 % v/v 4.7 2.9 U Direct Continuous 100 mM Tris-HCl assay 8.8 30Β°C 37.5 mM L-Phenylalanine Cinnamic acid β€” Incubation: ultrasonication (50 Hz/s), Assay: 100 rpm Water-incubated control (in U) | Bit of uncertainty about protein sequence, lyophilized enzyme incubation
Stability - Incubation Activity after incubation (1 hour) of lyophilized enzyme, measured by absorbance spectrophotometry (Cinnamic acid absorbance measurement, 290 nm) in aqueous phase 1-Butanol 100 % v/v 4.7 2.1 U Direct Continuous 100 mM Tris-HCl assay 8.8 30Β°C 37.5 mM L-Phenylalanine Cinnamic acid β€” Incubation: ultrasonication (50 Hz/s), Assay: 100 rpm Water-incubated control (in U) | Bit of uncertainty about protein sequence, lyophilized enzyme incubation
Stability - Incubation Activity after incubation (1 hour) of lyophilized enzyme, measured by absorbance spectrophotometry (Cinnamic acid absorbance measurement, 290 nm) in aqueous phase n-Hexane 100 % v/v 4.7 2.9 U Direct Continuous 100 mM Tris-HCl assay 8.8 30Β°C 37.5 mM L-Phenylalanine Cinnamic acid β€” Incubation: ultrasonication (50 Hz/s), Assay: 100 rpm Water-incubated control (in U) | Bit of uncertainty about protein sequence, lyophilized enzyme incubation
Stability - Incubation Activity after incubation (1 hour) of lyophilized enzyme, measured by absorbance spectrophotometry (Cinnamic acid absorbance measurement, 290 nm) in aqueous phase n-Heptane 100 % v/v 4.7 4.6 U Direct Continuous 100 mM Tris-HCl assay 8.8 30Β°C 37.5 mM L-Phenylalanine Cinnamic acid β€” Incubation: ultrasonication (50 Hz/s), Assay: 100 rpm Water-incubated control (in U) | Bit of uncertainty about protein sequence, lyophilized enzyme incubation
Stability - Incubation Activity after incubation (1 hour) of lyophilized enzyme, measured by absorbance spectrophotometry (Cinnamic acid absorbance measurement, 290 nm) in aqueous phase Benzene 100 % v/v 4.7 1.4 U Direct Continuous 100 mM Tris-HCl assay 8.8 30Β°C 37.5 mM L-Phenylalanine Cinnamic acid β€” Incubation: ultrasonication (50 Hz/s), Assay: 100 rpm Water-incubated control (in U) | Bit of uncertainty about protein sequence, lyophilized enzyme incubation
Stability - Incubation Activity after incubation (1 hour) of lyophilized enzyme, measured by absorbance spectrophotometry (Cinnamic acid absorbance measurement, 290 nm) in aqueous phase Toluene 100 % v/v 4.7 2.6 U Direct Continuous 100 mM Tris-HCl assay 8.8 30Β°C 37.5 mM L-Phenylalanine Cinnamic acid β€” Incubation: ultrasonication (50 Hz/s), Assay: 100 rpm Water-incubated control (in U) | Bit of uncertainty about protein sequence, lyophilized enzyme incubation
Stability - Incubation Activity after incubation (1 hour) of lyophilized enzyme, measured by absorbance spectrophotometry (Cinnamic acid absorbance measurement, 290 nm) in aqueous phase Methanol 100 % v/v 4.7 4.2 U Direct Continuous 100 mM Tris-HCl assay 8.8 30Β°C 37.5 mM L-Phenylalanine Cinnamic acid β€” 100 rpm Water-incubated control (in U) | Bit of uncertainty about protein sequence, lyophilized enzyme incubation
Stability - Incubation Activity after incubation (1 hour) of lyophilized enzyme, measured by absorbance spectrophotometry (Cinnamic acid absorbance measurement, 290 nm) in aqueous phase Ethanol 100 % v/v 4.25 4.1 U Direct Continuous 100 mM Tris-HCl assay 8.8 30Β°C 37.5 mM L-Phenylalanine methyl ester Cinnamic acid methyl ester β€” Incubation: ultrasonication (50 Hz/s), Assay: 100 rpm Water-incubated control (in U) | Bit of uncertainty about protein sequence, lyophilized enzyme incubation
Stability - Incubation Activity after incubation (1 hour) of lyophilized enzyme, measured by absorbance spectrophotometry (Cinnamic acid absorbance measurement, 290 nm) in aqueous phase Acetonitrile 100 % v/v 4.25 3.8 U Direct Continuous 100 mM Tris-HCl assay 8.8 30Β°C 37.5 mM L-Phenylalanine methyl ester Cinnamic acid methyl ester β€” Incubation: ultrasonication (50 Hz/s), Assay: 100 rpm Water-incubated control (in U) | Bit of uncertainty about protein sequence, lyophilized enzyme incubation
Stability - Incubation Activity after incubation (1 hour) of lyophilized enzyme, measured by absorbance spectrophotometry (Cinnamic acid absorbance measurement, 290 nm) in aqueous phase Acetone 100 % v/v 4.25 1.5 U Direct Continuous 100 mM Tris-HCl assay 8.8 30Β°C 37.5 mM L-Phenylalanine methyl ester Cinnamic acid methyl ester β€” Incubation: ultrasonication (50 Hz/s), Assay: 100 rpm Water-incubated control (in U) | Bit of uncertainty about protein sequence, lyophilized enzyme incubation
Stability - Incubation Activity after incubation (1 hour) of lyophilized enzyme, measured by absorbance spectrophotometry (Cinnamic acid absorbance measurement, 290 nm) in aqueous phase Dimethyl Sulfoxide (DMSO) 100 % v/v 4.25 2.8 U Direct Continuous 100 mM Tris-HCl assay 8.8 30Β°C 37.5 mM L-Phenylalanine methyl ester Cinnamic acid methyl ester β€” Incubation: ultrasonication (50 Hz/s), Assay: 100 rpm Water-incubated control (in U) | Bit of uncertainty about protein sequence, lyophilized enzyme incubation
Stability - Incubation Activity after incubation (1 hour) of lyophilized enzyme, measured by absorbance spectrophotometry (Cinnamic acid absorbance measurement, 290 nm) in aqueous phase 1-Butanol 100 % v/v 4.25 2.1 U Direct Continuous 100 mM Tris-HCl assay 8.8 30Β°C 37.5 mM L-Phenylalanine methyl ester Cinnamic acid methyl ester β€” Incubation: ultrasonication (50 Hz/s), Assay: 100 rpm Water-incubated control (in U) | Bit of uncertainty about protein sequence, lyophilized enzyme incubation
Stability - Incubation Activity after incubation (1 hour) of lyophilized enzyme, measured by absorbance spectrophotometry (Cinnamic acid absorbance measurement, 290 nm) in aqueous phase n-Hexane 100 % v/v 4.25 2.7 U Direct Continuous 100 mM Tris-HCl assay 8.8 30Β°C 37.5 mM L-Phenylalanine methyl ester Cinnamic acid methyl ester β€” Incubation: ultrasonication (50 Hz/s), Assay: 100 rpm Water-incubated control (in U) | Bit of uncertainty about protein sequence, lyophilized enzyme incubation
Stability - Incubation Activity after incubation (1 hour) of lyophilized enzyme, measured by absorbance spectrophotometry (Cinnamic acid absorbance measurement, 290 nm) in aqueous phase n-Heptane 100 % v/v 4.25 4.1 U Direct Continuous 100 mM Tris-HCl assay 8.8 30Β°C 37.5 mM L-Phenylalanine methyl ester Cinnamic acid methyl ester β€” Incubation: ultrasonication (50 Hz/s), Assay: 100 rpm Water-incubated control (in U) | Bit of uncertainty about protein sequence, lyophilized enzyme incubation
Stability - Incubation Activity after incubation (1 hour) of lyophilized enzyme, measured by absorbance spectrophotometry (Cinnamic acid absorbance measurement, 290 nm) in aqueous phase Benzene 100 % v/v 4.25 1.4 U Direct Continuous 100 mM Tris-HCl assay 8.8 30Β°C 37.5 mM L-Phenylalanine methyl ester Cinnamic acid methyl ester β€” Incubation: ultrasonication (50 Hz/s), Assay: 100 rpm Water-incubated control (in U) | Bit of uncertainty about protein sequence, lyophilized enzyme incubation
Stability - Incubation Activity after incubation (1 hour) of lyophilized enzyme, measured by absorbance spectrophotometry (Cinnamic acid absorbance measurement, 290 nm) in aqueous phase Toluene 100 % v/v 4.25 2.4 U Direct Continuous 100 mM Tris-HCl assay 8.8 30Β°C 37.5 mM L-Phenylalanine methyl ester Cinnamic acid methyl ester β€” Incubation: ultrasonication (50 Hz/s), Assay: 100 rpm Water-incubated control (in U) | Bit of uncertainty about protein sequence, lyophilized enzyme incubation
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Visualization : Stability β€” Incubation

One bar per measurement. Colour = solvent, shade = solvent volume.

Structure

🧬

No structure available for this protein.