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Literature summary extracted from

  • Blakley, E.R.
    The catabolism of L-tyrosine by an Arthrobacter sp. (1977), Can. J. Microbiol., 23, 1128-1139.
    View publication on PubMed

Activating Compound

EC Number Activating Compound Comment Organism Structure
1.2.3.13 2-mercaptoethanol
-
 Arthrobacter globiformis
1.2.3.13 cysteine
-
 Arthrobacter globiformis
1.2.3.13 dithiothreitol
-
 Arthrobacter globiformis
1.2.3.13 GSH optimal activity at 0.002 mM, can be replaced by 2-mercaptoethanol, cysteine or dithiothreitol Arthrobacter globiformis

General Stability

EC Number General Stability Organism
1.2.3.13 stabilizing effects of activity with ammonium sulfate, NaCl, Na2SO4 or MgSO4 Arthrobacter globiformis
1.13.11.15 dialysis against buffer for several hours at 0°C, no appreciable loss of activity Arthrobacter sp.

Inhibitors

EC Number Inhibitors Comment Organism Structure
1.2.3.13 EDTA potent inhibitor, other metal chelators ineffective Arthrobacter globiformis
1.14.14.9 EDTA inhibits non-purified enzyme, ammonium sulfate precipitate Arthrobacter sp.

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
1.2.3.13 Mg2+ optimal activity at 0.01 mM Arthrobacter globiformis
1.2.3.13 Mn2+ optimal activity at 0.01 mM Arthrobacter globiformis

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
1.2.1.16 succinate semialdehyde + NADP+ + H2O Arthrobacter sp. degradation of 3,4-dihydroxyphenylacetate in Arthrobacter sp. succinate + NADPH + H+
-
 ?
1.2.1.16 succinate semialdehyde + NADP+ + H2O Arthrobacter sp. PRL W15 degradation of 3,4-dihydroxyphenylacetate in Arthrobacter sp. succinate + NADPH + H+
-
 ?
1.2.1.60 5-carboxymethyl-2-hydroxymuconate semialdehyde + H2O + NAD+ Arthrobacter globiformis involved in the meta-cleavage pathway of 4-hydroxyphenylacetate 5-carboxymethyl-2-hydroxymuconate + NADH
-
 ?
1.2.1.60 5-carboxymethyl-2-hydroxymuconate semialdehyde + H2O + NAD+ Arthrobacter globiformis PRL W15 involved in the meta-cleavage pathway of 4-hydroxyphenylacetate 5-carboxymethyl-2-hydroxymuconate + NADH
-
 ?
1.2.3.13 4-hydroxyphenylpyruvate + O2 Arthrobacter globiformis
-
 4-hydroxyphenylacetate + CO2
-
 ?
1.2.3.13 4-hydroxyphenylpyruvate + O2 Arthrobacter globiformis PRL W15
-
 4-hydroxyphenylacetate + CO2
-
 ?
1.13.11.15 3,4-dihydroxyphenylacetate + O2 Arthrobacter sp. enzyme is involved in catabolism of L-Tyr 2-hydroxy-5-carboxymethylmuconate semialdehyde
-
 ?
1.14.14.9 4-hydroxyphenylacetate + NADH + O2 Arthrobacter sp. degradation of tyrosine with 3,4-dihydroxyphenylacetate as key intermediate 3,4-dihydroxyphenylacetate + NAD+ + H2O
-
 ?
1.14.14.9 4-hydroxyphenylacetate + NADH + O2 Arthrobacter sp. PRL W15 degradation of tyrosine with 3,4-dihydroxyphenylacetate as key intermediate 3,4-dihydroxyphenylacetate + NAD+ + H2O
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
1.2.1.16 Arthrobacter sp.
-
-
-
1.2.1.60 Arthrobacter globiformis
-
-
-
1.2.1.60 Arthrobacter globiformis PRL W15
-
-
-
1.2.3.13 Arthrobacter globiformis
-
-
-
1.13.11.15 Arthrobacter sp.
-
-
-
1.14.14.9 Arthrobacter sp.
-
 PRL W15
-
1.14.14.9 Arthrobacter sp. PRL W15
-
 PRL W15
-

Purification (Commentary)

EC Number Purification (Comment) Organism
1.14.14.9 ultracentrifugation, ammonium sulfate precipitation Arthrobacter sp.

Source Tissue

EC Number Source Tissue Comment Organism Textmining
1.2.1.60 cell culture
-
 Arthrobacter globiformis
-
1.2.3.13 culture condition:L-tyrosine-grown cell
-
 Arthrobacter globiformis
-

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
1.2.1.16 additional information
-
-
 Arthrobacter sp.
1.14.14.9 additional information
-
 activity is reduced by about 40% if 3-hydroxyphenylacetate is used as substrate instead of 4-hydroxyphenylacetate Arthrobacter sp.

Storage Stability

EC Number Storage Stability Organism
1.2.3.13 -20°C, ammonium sulfate precipitation or crude extract, 4 weeks Arthrobacter globiformis
1.13.11.15 10°C, lyophilized preparations of the enzyme, 8 months, stable Arthrobacter sp.

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.2.1.16 succinate semialdehyde + NADP+ + H2O
-
 Arthrobacter sp. succinate + NADPH + H+
-
 ?
1.2.1.16 succinate semialdehyde + NADP+ + H2O degradation of 3,4-dihydroxyphenylacetate in Arthrobacter sp. Arthrobacter sp. succinate + NADPH + H+
-
 ?
1.2.1.16 succinate semialdehyde + NADP+ + H2O
-
 Arthrobacter sp. PRL W15 succinate + NADPH + H+
-
 ?
1.2.1.16 succinate semialdehyde + NADP+ + H2O degradation of 3,4-dihydroxyphenylacetate in Arthrobacter sp. Arthrobacter sp. PRL W15 succinate + NADPH + H+
-
 ?
1.2.1.60 5-carboxymethyl-2-hydroxymuconate semialdehyde + H2O + NAD+ involved in the meta-cleavage pathway of 4-hydroxyphenylacetate Arthrobacter globiformis 5-carboxymethyl-2-hydroxymuconate + NADH
-
 ?
1.2.1.60 5-carboxymethyl-2-hydroxymuconate semialdehyde + H2O + NAD+ involved in the meta-cleavage pathway of 4-hydroxyphenylacetate Arthrobacter globiformis PRL W15 5-carboxymethyl-2-hydroxymuconate + NADH
-
 ?
1.2.3.13 4-hydroxyphenylpyruvate + O2
-
 Arthrobacter globiformis 4-hydroxyphenylacetate + CO2
-
 ?
1.2.3.13 4-hydroxyphenylpyruvate + O2
-
 Arthrobacter globiformis PRL W15 4-hydroxyphenylacetate + CO2
-
 ?
1.2.3.13 glyoxylate + O2 19% of the activity compared to 4-hydroxyphenylpyruvate as substrate Arthrobacter globiformis CO2 + CO2
-
 ?
1.2.3.13 glyoxylate + O2 19% of the activity compared to 4-hydroxyphenylpyruvate as substrate Arthrobacter globiformis PRL W15 CO2 + CO2
-
 ?
1.2.3.13 phenylpyruvate + O2 84% of the activity compared to 4-hydroxyphenylpyruvate as substrate Arthrobacter globiformis phenylacetate + CO2
-
 ?
1.2.3.13 phenylpyruvate + O2 84% of the activity compared to 4-hydroxyphenylpyruvate as substrate Arthrobacter globiformis PRL W15 phenylacetate + CO2
-
 ?
1.13.11.15 3,4-dihydroxyphenylacetate + O2
-
 Arthrobacter sp. 2-hydroxy-5-carboxymethylmuconate semialdehyde
-
 ?
1.13.11.15 3,4-dihydroxyphenylacetate + O2 enzyme is involved in catabolism of L-Tyr Arthrobacter sp. 2-hydroxy-5-carboxymethylmuconate semialdehyde
-
 ?
1.14.14.9 3-hydroxyphenylacetate + NAD(P)H + O2
-
 Arthrobacter sp. 3,4-hydroxyphenylacetate + NAD(P)+ + H2O
-
 ?
1.14.14.9 3-hydroxyphenylacetate + NAD(P)H + O2
-
 Arthrobacter sp. PRL W15 3,4-hydroxyphenylacetate + NAD(P)+ + H2O
-
 ?
1.14.14.9 4-hydroxyphenylacetate + NAD(P)H + O2 enzyme is induced by 4-hydroxyphenylacetate, no constitutive synthesis Arthrobacter sp. 3,4-dihydroxyphenylacetate + NAD(P)+ + H2O
-
 ir
1.14.14.9 4-hydroxyphenylacetate + NAD(P)H + O2 enzyme is induced by 4-hydroxyphenylacetate, no constitutive synthesis Arthrobacter sp. PRL W15 3,4-dihydroxyphenylacetate + NAD(P)+ + H2O
-
 ir
1.14.14.9 4-hydroxyphenylacetate + NADH + O2 degradation of tyrosine with 3,4-dihydroxyphenylacetate as key intermediate Arthrobacter sp. 3,4-dihydroxyphenylacetate + NAD+ + H2O
-
 ?
1.14.14.9 4-hydroxyphenylacetate + NADH + O2 degradation of tyrosine with 3,4-dihydroxyphenylacetate as key intermediate Arthrobacter sp. PRL W15 3,4-dihydroxyphenylacetate + NAD+ + H2O
-
 ?

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
1.14.14.9 28
-
 assay at Arthrobacter sp.

Temperature Stability [°C]

EC Number Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
1.2.3.13
-
-
 10% loss of activity per h Arthrobacter globiformis
1.13.11.15 55
-
 5 min, stable Arthrobacter sp.

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
1.2.3.13 7.5
-
-
 Arthrobacter globiformis
1.14.14.9 7.5
-
 assay at Arthrobacter sp.

Cofactor

EC Number Cofactor Comment Organism Structure
1.2.1.16 NAD+ rate with NADP+ is about twice that with NAD+, crude extract Arthrobacter sp.
1.2.1.16 NADP+ rate with NADP+ is about twice that with NAD+, crude extract Arthrobacter sp.
1.2.1.60 NAD+ can not be replaced by NADP+ Arthrobacter globiformis
1.2.3.13 FAD optimal activity at 10 nM, can not be replaced by NAD+, NADP+ or FMN Arthrobacter globiformis
1.2.3.13 thiamine diphosphate optimal activity at 0.004 mM, absolute requirement Arthrobacter globiformis
1.14.14.9 additional information similar enzyme which oxidizes both NADH and NADPH Arthrobacter sp.