Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary extracted from

  • Trautwein-Schult, A.; Jankowska, D.; Cordes, A.; Hoferichter, P.; Klein, C.; Matros, A.; Mock, H.P.; Baronian, K.; Bode, R.; Kunze, G.
    Arxula adeninivorans recombinant guanine deaminase and its application in the production of food with low purine content (2014), J. Mol. Microbiol. Biotechnol., 24, 67-81.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
3.5.4.3 expressed in Arxula adeninivorans strain G1212 Blastobotrys adeninivorans

Inhibitors

EC Number Inhibitors Comment Organism Structure
3.5.4.3 additional information not inhibited by EDTA, 1,10-phenanthroline, dithiothreitol, L-cysteine, and phenylmethylsulfonyl fluoride Blastobotrys adeninivorans

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
3.5.4.3 0.026
-
guanine recombinant enzyme, at pH 6.0 and 37°C Blastobotrys adeninivorans
3.5.4.3 0.056
-
guanine native enzyme, at pH 6.0 and 37°C Blastobotrys adeninivorans

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
3.5.4.3 cytoplasm
-
Blastobotrys adeninivorans 5737
-
3.5.4.3 vacuole
-
Blastobotrys adeninivorans 5773
-

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
3.5.4.3 Cu2+ at 1 mM Cu2+, the native enzyme shows about 80% inhibition and the recombinant enzyme almost complete (99%) inhibition Blastobotrys adeninivorans
3.5.4.3 Hg2+ complete inhibition at 1 mM Blastobotrys adeninivorans
3.5.4.3 additional information not influenced by Ca2+, Fe3+, K+, Mg2+, Ni2+, and Zn2+ Blastobotrys adeninivorans

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
3.5.4.3 53000
-
2 * 53000, calculated from amino acid sequence Blastobotrys adeninivorans
3.5.4.3 55000
-
2 * 55000, SDS-PAGE and MALDI-TOF mass spectrometry Blastobotrys adeninivorans
3.5.4.3 100000 110000 recombinant and native enzyme, gel filtration Blastobotrys adeninivorans

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
3.5.4.3 guanine + H2O Blastobotrys adeninivorans 100% activity xanthine + NH3
-
r
3.5.4.3 guanine + H2O Blastobotrys adeninivorans LS3 100% activity xanthine + NH3
-
r

Organism

EC Number Organism UniProt Comment Textmining
3.5.4.3 Blastobotrys adeninivorans
-
-
-
3.5.4.3 Blastobotrys adeninivorans LS3
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
3.5.4.3 heat precipitation, DEAE Sepharose column chromatography, and Superdex 200 gel filtration Blastobotrys adeninivorans

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
3.5.4.3 0.1
-
crude extract, at pH 6.0 and 37°C Blastobotrys adeninivorans
3.5.4.3 4.7
-
after 51.5fold purification, at pH 6.0 and 37°C Blastobotrys adeninivorans

Storage Stability

EC Number Storage Stability Organism
3.5.4.3 -20°C, 28 days, 123% activity Blastobotrys adeninivorans
3.5.4.3 -20°C, with 20% (v/v) glycine, 28 days, 65% residual activity Blastobotrys adeninivorans
3.5.4.3 22°C, 28 days, 34% residual activity Blastobotrys adeninivorans
3.5.4.3 4°C, 28 days, 44% residual activity Blastobotrys adeninivorans

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.5.4.3 2,6-diaminopurine + H2O the native enzyme shows 107% activity and the recombinant enzyme 98% activity compared to guanine Blastobotrys adeninivorans ?
-
?
3.5.4.3 2-amino-6-chloropurine + H2O the native enzyme shows 93% activity and the recombinant enzyme 88% activity compared to guanine Blastobotrys adeninivorans 6-chloro-9H-purin-2-ol + NH3
-
?
3.5.4.3 8-azaguanine + H2O the native enzyme shows 99% activity and the recombinant enzyme 95% activity compared to guanine Blastobotrys adeninivorans 8-azaxanthine + NH3
-
?
3.5.4.3 8-azaguanine + H2O the native enzyme shows 99% activity and the recombinant enzyme 95% activity compared to guanine Blastobotrys adeninivorans LS3 8-azaxanthine + NH3
-
?
3.5.4.3 8-azaxanthine + H2O the native enzyme shows 95% activity and the recombinant enzyme 88% activity compared to guanine Blastobotrys adeninivorans ?
-
?
3.5.4.3 adenine + H2O the native enzyme shows 102% activity and the recombinant enzyme 85% activity compared to guanine Blastobotrys adeninivorans allopurinol + NH3
-
?
3.5.4.3 adenine + H2O the native enzyme shows 102% activity and the recombinant enzyme 85% activity compared to guanine Blastobotrys adeninivorans LS3 allopurinol + NH3
-
?
3.5.4.3 adenosine + H2O the native enzyme shows 98% activity and the recombinant enzyme 91% activity compared to guanine Blastobotrys adeninivorans inosine + NH3
-
?
3.5.4.3 adenosine + H2O the native enzyme shows 98% activity and the recombinant enzyme 91% activity compared to guanine Blastobotrys adeninivorans LS3 inosine + NH3
-
?
3.5.4.3 guanine + H2O 100% activity Blastobotrys adeninivorans xanthine + NH3
-
r
3.5.4.3 guanine + H2O 100% activity Blastobotrys adeninivorans LS3 xanthine + NH3
-
r
3.5.4.3 guanosine + H2O the native enzyme shows 48% activity and the recombinant enzyme 70% activity compared to guanine Blastobotrys adeninivorans ?
-
?
3.5.4.3 hypoxanthine + H2O the native enzyme shows 100% activity and the recombinant enzyme 87% activity compared to guanine Blastobotrys adeninivorans ?
-
?
3.5.4.3 uric acid + H2O the native enzyme shows 89% activity and the recombinant enzyme 86% activity compared to guanine Blastobotrys adeninivorans ?
-
?
3.5.4.3 uric acid + H2O the native enzyme shows 89% activity and the recombinant enzyme 86% activity compared to guanine Blastobotrys adeninivorans LS3 ?
-
?
3.5.4.3 xanthine + H2O the native enzyme shows 01% activity and the recombinant enzyme 87% activity compared to guanine Blastobotrys adeninivorans ?
-
?

Subunits

EC Number Subunits Comment Organism
3.5.4.3 homodimer 2 * 53000, calculated from amino acid sequence Blastobotrys adeninivorans
3.5.4.3 homodimer 2 * 55000, SDS-PAGE and MALDI-TOF mass spectrometry Blastobotrys adeninivorans

Synonyms

EC Number Synonyms Comment Organism
3.5.4.3 Agdap
-
Blastobotrys adeninivorans
3.5.4.3 GDA
-
Blastobotrys adeninivorans
3.5.4.3 Guanine aminohydrolase
-
Blastobotrys adeninivorans

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
3.5.4.3 55
-
-
Blastobotrys adeninivorans

Temperature Stability [°C]

EC Number Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
3.5.4.3 30
-
the native enzyme remains stable for 1 h at up to 30°C Blastobotrys adeninivorans
3.5.4.3 60
-
the recombinant enzyme remains stable for 1 h at up to 60°C Blastobotrys adeninivorans

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
3.5.4.3 1.5
-
guanine recombinant enzyme, at pH 6.0 and 37°C Blastobotrys adeninivorans
3.5.4.3 3.9
-
guanine native enzyme, at pH 6.0 and 37°C Blastobotrys adeninivorans

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
3.5.4.3 6.5
-
the native enzyme shows optimal pH values of 6.5 and 8.0 while the recombinant enzyme has a single pH optimum at pH 6.5 Blastobotrys adeninivorans
3.5.4.3 8
-
the native enzyme shows optimal pH values of 6.5 and 8.0 Blastobotrys adeninivorans

pH Stability

EC Number pH Stability pH Stability Maximum Comment Organism
3.5.4.3 6.5 8 native and recombinant enzymes are stable during incubation for 1 h at 37°C with pH in the range of 6.5-8.0 Blastobotrys adeninivorans

pI Value

EC Number Organism Comment pI Value Maximum pI Value
3.5.4.3 Blastobotrys adeninivorans calculated from amino acid sequence
-
5.7

Expression

EC Number Organism Comment Expression
3.5.4.3 Blastobotrys adeninivorans immediately after the shift of cells into media with purine as nitrogen source, the enzyme transcript level increases and reached maximum level at 2 h with adenine and 4 h with hypoxanthine, after which transcription fell to the basal level up