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Literature summary extracted from

  • Izumi, Y.; Morita, H.; Tani, Y.; Ogata, K.
    The pimelyl-CoA synthetase responsible for the first step in biotin biosynthesis by microorganisms (1974), Agric. Biol. Chem., 38, 2257-2262.
No PubMed abstract available

Inhibitors

EC Number Inhibitors Comment Organism Structure
6.2.1.14 1,10-phenanthroline
-
Lysinibacillus sphaericus
6.2.1.14 1,10-phenanthroline
-
Priestia megaterium
6.2.1.14 2,2'-dipyridyl
-
Priestia megaterium
6.2.1.14 Al3+
-
Priestia megaterium
6.2.1.14 EDTA
-
Lysinibacillus sphaericus
6.2.1.14 EDTA
-
Priestia megaterium
6.2.1.14 Fe2+
-
Priestia megaterium
6.2.1.14 Fe3+
-
Priestia megaterium
6.2.1.14 iodoacetic acid
-
Priestia megaterium
6.2.1.14 Mg2+ inhibition above 10 mM, requirement at lower concentrations Lysinibacillus sphaericus
6.2.1.14 Mg2+ inhibition above 10 mM, requirement at lower concentrations Priestia megaterium
6.2.1.14 p-chloromercuribenzoate
-
Priestia megaterium

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
6.2.1.14 0.27
-
heptanedioate
-
Priestia megaterium
6.2.1.14 0.55
-
CoA
-
Priestia megaterium
6.2.1.14 1.5
-
ATP
-
Priestia megaterium

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
6.2.1.14 Mg2+ required Priestia megaterium
6.2.1.14 Mg2+ required Lysinibacillus sphaericus
6.2.1.14 Mg2+ required Kocuria rosea
6.2.1.14 Mg2+ inhibition above 10 mM Priestia megaterium
6.2.1.14 Mg2+ inhibition above 10 mM Lysinibacillus sphaericus
6.2.1.14 Mg2+ Km: 1.5 mM Priestia megaterium
6.2.1.14 Mn2+
-
Lysinibacillus sphaericus
6.2.1.14 Mn2+ activates with 50% higher efficiency than Mg2+ Priestia megaterium

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
6.2.1.14 ATP + heptanedioate + CoA Bacillus subtilis
-
?
-
?
6.2.1.14 ATP + heptanedioate + CoA Priestia megaterium enzyme is responsible for the first step in biotin biosynthesis by microorganisms ?
-
?
6.2.1.14 ATP + heptanedioate + CoA Priestia megaterium NIHB 12 enzyme is responsible for the first step in biotin biosynthesis by microorganisms ?
-
?
6.2.1.14 ATP + heptanedioate + CoA Bacillus subtilis IAM 1193
-
?
-
?

Organism

EC Number Organism UniProt Comment Textmining
6.2.1.14 Bacillus subtilis
-
weak activity
-
6.2.1.14 Bacillus subtilis IAM 1193
-
weak activity
-
6.2.1.14 Devosia riboflavina
-
-
-
6.2.1.14 Devosia riboflavina IFO 3140
-
-
-
6.2.1.14 Enterobacter cloacae
-
-
-
6.2.1.14 Enterobacter cloacae IAM 1221
-
-
-
6.2.1.14 Escherichia coli
-
strain AKU 0007
-
6.2.1.14 Klebsiella aerogenes
-
strain AKU 0022, strain IFO 3317, strain IFO 12010
-
6.2.1.14 Kocuria rosea
-
-
-
6.2.1.14 Kocuria rosea IAM 1257
-
-
-
6.2.1.14 Kocuria rosea IFO 3764
-
-
-
6.2.1.14 Lysinibacillus sphaericus
-
-
-
6.2.1.14 Lysinibacillus sphaericus
-
weak
-
6.2.1.14 Lysinibacillus sphaericus IFO 3525
-
-
-
6.2.1.14 Priestia megaterium
-
-
-
6.2.1.14 Priestia megaterium NIHB 12
-
-
-
6.2.1.14 Pseudomonas fluorescens
-
-
-
6.2.1.14 Pseudomonas fluorescens AKU 0821
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
6.2.1.14 partial Priestia megaterium

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
6.2.1.14 additional information
-
-
Priestia megaterium

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
6.2.1.14 ADP + heptanedioate + CoA 85% of the activity relative to ATP Priestia megaterium AMP + phosphate + heptanedioyl-CoA
-
?
6.2.1.14 ADP + heptanedioate + CoA 85% of the activity relative to ATP Priestia megaterium NIHB 12 AMP + phosphate + heptanedioyl-CoA
-
?
6.2.1.14 ATP + heptanedioate + CoA
-
Bacillus subtilis AMP + diphosphate + heptanedioyl-CoA heptanedioyl-CoA i.e. pimelyl-CoA ?
6.2.1.14 ATP + heptanedioate + CoA
-
Escherichia coli AMP + diphosphate + heptanedioyl-CoA heptanedioyl-CoA i.e. pimelyl-CoA ?
6.2.1.14 ATP + heptanedioate + CoA
-
Enterobacter cloacae AMP + diphosphate + heptanedioyl-CoA heptanedioyl-CoA i.e. pimelyl-CoA ?
6.2.1.14 ATP + heptanedioate + CoA
-
Priestia megaterium AMP + diphosphate + heptanedioyl-CoA heptanedioyl-CoA i.e. pimelyl-CoA ?
6.2.1.14 ATP + heptanedioate + CoA
-
Lysinibacillus sphaericus AMP + diphosphate + heptanedioyl-CoA heptanedioyl-CoA i.e. pimelyl-CoA ?
6.2.1.14 ATP + heptanedioate + CoA
-
Kocuria rosea AMP + diphosphate + heptanedioyl-CoA heptanedioyl-CoA i.e. pimelyl-CoA ?
6.2.1.14 ATP + heptanedioate + CoA
-
Pseudomonas fluorescens AMP + diphosphate + heptanedioyl-CoA heptanedioyl-CoA i.e. pimelyl-CoA ?
6.2.1.14 ATP + heptanedioate + CoA
-
Klebsiella aerogenes AMP + diphosphate + heptanedioyl-CoA heptanedioyl-CoA i.e. pimelyl-CoA ?
6.2.1.14 ATP + heptanedioate + CoA
-
Devosia riboflavina AMP + diphosphate + heptanedioyl-CoA heptanedioyl-CoA i.e. pimelyl-CoA ?
6.2.1.14 ATP + heptanedioate + CoA
-
Enterobacter cloacae IAM 1221 AMP + diphosphate + heptanedioyl-CoA heptanedioyl-CoA i.e. pimelyl-CoA ?
6.2.1.14 ATP + heptanedioate + CoA
-
Pseudomonas fluorescens AKU 0821 AMP + diphosphate + heptanedioyl-CoA heptanedioyl-CoA i.e. pimelyl-CoA ?
6.2.1.14 ATP + heptanedioate + CoA
-
Priestia megaterium NIHB 12 AMP + diphosphate + heptanedioyl-CoA heptanedioyl-CoA i.e. pimelyl-CoA ?
6.2.1.14 ATP + heptanedioate + CoA
-
Kocuria rosea IFO 3764 AMP + diphosphate + heptanedioyl-CoA heptanedioyl-CoA i.e. pimelyl-CoA ?
6.2.1.14 ATP + heptanedioate + CoA
-
Lysinibacillus sphaericus IFO 3525 AMP + diphosphate + heptanedioyl-CoA heptanedioyl-CoA i.e. pimelyl-CoA ?
6.2.1.14 ATP + heptanedioate + CoA
-
Kocuria rosea IAM 1257 AMP + diphosphate + heptanedioyl-CoA heptanedioyl-CoA i.e. pimelyl-CoA ?
6.2.1.14 ATP + heptanedioate + CoA
-
Bacillus subtilis IAM 1193 AMP + diphosphate + heptanedioyl-CoA heptanedioyl-CoA i.e. pimelyl-CoA ?
6.2.1.14 ATP + heptanedioate + CoA
-
Devosia riboflavina IFO 3140 AMP + diphosphate + heptanedioyl-CoA heptanedioyl-CoA i.e. pimelyl-CoA ?
6.2.1.14 ATP + heptanedioate + CoA
-
Bacillus subtilis ?
-
?
6.2.1.14 ATP + heptanedioate + CoA enzyme is responsible for the first step in biotin biosynthesis by microorganisms Priestia megaterium ?
-
?
6.2.1.14 ATP + heptanedioate + CoA enzyme is responsible for the first step in biotin biosynthesis by microorganisms Priestia megaterium NIHB 12 ?
-
?
6.2.1.14 ATP + heptanedioate + CoA
-
Bacillus subtilis IAM 1193 ?
-
?

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
6.2.1.14 32
-
-
Priestia megaterium

Temperature Range [°C]

EC Number Temperature Minimum [°C] Temperature Maximum [°C] Comment Organism
6.2.1.14 15 52 15°C: about 50% of maximal activity, 52°C: about 15% of maximal activity Priestia megaterium

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
6.2.1.14 8
-
Tris-HCl buffer Priestia megaterium