BRENDA - Enzyme Database show
show all sequences of 6.2.1.11

Formation of biotinyl-CoA synthetase, the first enzyme involved in microbial biotin degradation

Yamada, H.; Osakai, M.; Izumi, Y.; Agric. Biol. Chem. 48, 2039-2045 (1984)
No PubMed abstract available

Data extracted from this reference:

Metals/Ions
Metals/Ions
Commentary
Organism
Structure
Mg2+
required
Mycoplana sp.
Mn2+
can replace Mg2+
Mycoplana sp.
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Mycoplana sp.
-
No. 166
-
Mycoplana sp. No. 166
-
No. 166
-
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
ATP + biotin + CoA
-
591
Mycoplana sp.
AMP + diphosphate + biotinyl-CoA
-
591
Mycoplana sp.
-
ATP + biotin + CoA
-
591
Mycoplana sp. No. 166
AMP + diphosphate + biotinyl-CoA
-
591
Mycoplana sp. No. 166
-
ATP + dethiobiotin + CoA
26% of the activity relative to biotin
591
Mycoplana sp.
AMP + diphosphate + dethiobiotinyl-CoA
-
-
-
-
ATP + dethiobiotin + CoA
26% of the activity relative to biotin
591
Mycoplana sp. No. 166
AMP + diphosphate + dethiobiotinyl-CoA
-
-
-
-
Metals/Ions (protein specific)
Metals/Ions
Commentary
Organism
Structure
Mg2+
required
Mycoplana sp.
Mn2+
can replace Mg2+
Mycoplana sp.
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
ATP + biotin + CoA
-
591
Mycoplana sp.
AMP + diphosphate + biotinyl-CoA
-
591
Mycoplana sp.
-
ATP + biotin + CoA
-
591
Mycoplana sp. No. 166
AMP + diphosphate + biotinyl-CoA
-
591
Mycoplana sp. No. 166
-
ATP + dethiobiotin + CoA
26% of the activity relative to biotin
591
Mycoplana sp.
AMP + diphosphate + dethiobiotinyl-CoA
-
-
-
-
ATP + dethiobiotin + CoA
26% of the activity relative to biotin
591
Mycoplana sp. No. 166
AMP + diphosphate + dethiobiotinyl-CoA
-
-
-
-
Other publictions for EC 6.2.1.11
No.
1st author
Pub Med
title
organims
journal
volume
pages
year
Activating Compound
Application
Cloned(Commentary)
Crystallization (Commentary)
Engineering
General Stability
Inhibitors
KM Value [mM]
Localization
Metals/Ions
Molecular Weight [Da]
Natural Substrates/ Products (Substrates)
Organic Solvent Stability
Organism
Oxidation Stability
Posttranslational Modification
Purification (Commentary)
Reaction
Renatured (Commentary)
Source Tissue
Specific Activity [micromol/min/mg]
Storage Stability
Substrates and Products (Substrate)
Subunits
Temperature Optimum [°C]
Temperature Range [°C]
Temperature Stability [°C]
Turnover Number [1/s]
pH Optimum
pH Range
pH Stability
Cofactor
Ki Value [mM]
pI Value
IC50 Value
Activating Compound (protein specific)
Application (protein specific)
Cloned(Commentary) (protein specific)
Cofactor (protein specific)
Crystallization (Commentary) (protein specific)
Engineering (protein specific)
General Stability (protein specific)
IC50 Value (protein specific)
Inhibitors (protein specific)
Ki Value [mM] (protein specific)
KM Value [mM] (protein specific)
Localization (protein specific)
Metals/Ions (protein specific)
Molecular Weight [Da] (protein specific)
Natural Substrates/ Products (Substrates) (protein specific)
Organic Solvent Stability (protein specific)
Oxidation Stability (protein specific)
Posttranslational Modification (protein specific)
Purification (Commentary) (protein specific)
Renatured (Commentary) (protein specific)
Source Tissue (protein specific)
Specific Activity [micromol/min/mg] (protein specific)
Storage Stability (protein specific)
Substrates and Products (Substrate) (protein specific)
Subunits (protein specific)
Temperature Optimum [°C] (protein specific)
Temperature Range [°C] (protein specific)
Temperature Stability [°C] (protein specific)
Turnover Number [1/s] (protein specific)
pH Optimum (protein specific)
pH Range (protein specific)
pH Stability (protein specific)
pI Value (protein specific)
Expression
General Information
General Information (protein specific)
Expression (protein specific)
KCat/KM [mM/s]
KCat/KM [mM/s] (protein specific)
589
Tanaka
-
Microbial metabolism and produ ...
Mycoplana sp., Mycoplana sp. No. 166
Vitamins (Kyoto)
62
305-315
1988
-
-
-
-
-
-
8
6
-
2
1
-
-
3
-
-
1
-
-
-
-
-
8
1
1
-
-
-
1
-
1
-
-
-
-
-
-
-
-
-
-
-
-
8
-
6
-
2
1
-
-
-
-
1
-
-
-
-
8
1
1
-
-
-
1
-
1
-
-
-
-
-
-
-
593
Tanaka
-
Enzymatic production of alpha- ...
Mycoplana sp.
J. Biotechnol.
5
209-220
1987
-
1
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
594
Tanaka
-
Enzymatic assay for biotin usi ...
Mycoplana sp.
Agric. Biol. Chem.
51
2585-2586
1987
-
1
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
592
Tanaka
Purification and properties of ...
Mycoplana sp.
Arch. Biochem. Biophys.
251
479-486
1986
-
-
-
-
-
-
9
5
-
2
1
1
-
3
-
-
1
-
-
-
1
-
9
1
1
-
7
-
1
-
1
-
-
-
-
-
-
-
-
-
-
-
-
9
-
5
-
2
1
1
-
-
-
1
-
-
1
-
9
1
1
-
7
-
1
-
1
-
-
-
-
-
-
-
591
Yamada
-
Formation of biotinyl-CoA synt ...
Mycoplana sp., Mycoplana sp. No. 166
Agric. Biol. Chem.
48
2039-2045
1984
-
-
-
-
-
-
-
-
-
2
-
-
-
3
-
-
-
-
-
-
-
-
4
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
2
-
-
-
-
-
-
-
-
-
-
4
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
590
Christner
Enzymatic activation of biotin ...
Soil bacterium, Sus scrofa
J. Biol. Chem.
239
3997-4005
1964
-
-
-
-
-
1
-
-
-
1
-
-
-
2
-
-
1
-
-
1
1
1
2
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
1
-
-
-
-
-
1
-
1
1
1
2
-
-
-
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