Information on EC 2.3.1.47 - 8-amino-7-oxononanoate synthase

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The expected taxonomic range for this enzyme is: Bacteria, Eukaryota

EC NUMBER
COMMENTARY
2.3.1.47
-
RECOMMENDED NAME
GeneOntology No.
8-amino-7-oxononanoate synthase
-
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
pimeloyl-[acyl-carrier protein] + L-alanine = 8-amino-7-oxononanoate + CO2 + holo-[acyl-carrier protein]
show the reaction diagram
reaction mechanism; reaction mechanism could be shared by all alpha-oxoamine synthases; reaction mechanism, formation of the pyridoxal-phosphate-stabilized carbanion by abstraction of the C2-H proton of the alanine-pyridoxal-phosphate aldimine, followed by acylation and decarboxylation
-
pimeloyl-[acyl-carrier protein] + L-alanine = 8-amino-7-oxononanoate + CO2 + holo-[acyl-carrier protein]
show the reaction diagram
binding of pimeloyl-CoA causes a conformational change in the active site; binding study of L-alanine and D-alanine to the enzyme; Schiff base formation between D- or L-alanine and pyridoxal-5'-phophate in the active site
-
pimeloyl-[acyl-carrier protein] + L-alanine = 8-amino-7-oxononanoate + CO2 + holo-[acyl-carrier protein]
show the reaction diagram
reaction mechanism; reaction mechanism, formation of the pyridoxal-phosphate-stabilized carbanion by abstraction of the C2-H proton of the alanine-pyridoxal-phosphate aldimine, followed by acylation and decarboxylation
-
pimeloyl-[acyl-carrier protein] + L-alanine = 8-amino-7-oxononanoate + CO2 + holo-[acyl-carrier protein]
show the reaction diagram
reaction mechanism
-
pimeloyl-[acyl-carrier protein] + L-alanine = 8-amino-7-oxononanoate + CO2 + holo-[acyl-carrier protein]
show the reaction diagram
binding study of L-alanine and D-alanine to the enzyme; reaction mechanism
-
pimeloyl-[acyl-carrier protein] + L-alanine = 8-amino-7-oxononanoate + CO2 + holo-[acyl-carrier protein]
show the reaction diagram
analysis of the reaction mechanism via an enzyme-bound intermediate beta-ketoacid pyridoxal-5'-phosphate aldimine, presence of multiple catalytic residues in the Escherichia coli enzyme
-
pimeloyl-[acyl-carrier protein] + L-alanine = 8-amino-7-oxononanoate + CO2 + holo-[acyl-carrier protein]
show the reaction diagram
formation of an external intermediate beta-ketoacid pyridoxal-5'-phosphate aldimine, preference for L-alanine
-
pimeloyl-[acyl-carrier protein] + L-alanine = 8-amino-7-oxononanoate + CO2 + holo-[acyl-carrier protein]
show the reaction diagram
detailed catalytic reaction mechanism, overview
-
pimeloyl-[acyl-carrier protein] + L-alanine = 8-amino-7-oxononanoate + CO2 + holo-[acyl-carrier protein]
show the reaction diagram
via an AtbioF-PLP internal aldimine complex, i.e. a Schiff base formed between PLP and a Lys residue in the protein
pimeloyl-[acyl-carrier protein] + L-alanine = 8-amino-7-oxononanoate + CO2 + holo-[acyl-carrier protein]
show the reaction diagram
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Acyl group transfer
-
-
-
-
Claisen condensation
-
-
decarboxylation
-
-
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
8-amino-7-oxononanoate biosynthesis I
-
-
8-amino-7-oxononanoate biosynthesis II
-
-
8-amino-7-oxononanoate biosynthesis III
-
-
biotin biosynthesis
-
-
Biotin metabolism
-
-
Metabolic pathways
-
-
Microbial metabolism in diverse environments
-
-
SYSTEMATIC NAME
IUBMB Comments
6-carboxyhexanoyl-[acyl-carrier protein]:L-alanine C-carboxyhexanoyltransferase (decarboxylating)
A pyridoxal-phosphate protein. The enzyme catalyses the decarboxylative condensation of L-alanine and pimeloyl-[acyl-carrier protein], a key step in the pathway for biotin biosynthesis. Pimeloyl-CoA can be used with lower efficiency [5].
SYNONYMS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7,8-diaminopelargonic acid aminotransferase
-
-
7,8-diaminopelargonic acid aminotransferase
Escherichia coli C268
-
-
-
7,8-diaminopelargonic acid aminotransferase
-
-
7-KAP synthetase
-
-
7-keto-8-aminopelargonate synthetase
-
-
-
-
7-keto-8-aminopelargonic acid synthase
-
-
7-keto-8-aminopelargonic acid synthase
-
-
7-keto-8-aminopelargonic acid synthase
-
7-keto-8-aminopelargonic acid synthase
-
-
7-keto-8-aminopelargonic acid synthase
Geobacillus kaustophilus JCM12893
-
-
-
7-keto-8-aminopelargonic acid synthase
-
-
7-keto-8-aminopelargonic acid synthase
-
-
7-keto-8-aminopelargonic acid synthase
Ruminiclostridium thermocellum ATCC27405
-
-
-
7-keto-8-aminopelargonic acid synthase
-
-
7-keto-8-aminopelargonic acid synthase
Symbiobacterium thermophilum IAM14863
-
-
-
7-keto-8-aminopelargonic acid synthase
-
-
7-keto-8-aminopelargonic acid synthetase
-
-
-
-
7-keto-8-aminopelargonic synthetase
-
-
-
-
7-oxo-8-aminononanoate synthase
-
-
-
-
8-amino-7-oxononanoate synthase
-
-
8-amino-7-oxononanoate synthase
-
-
8-amino-7-oxononanoate synthase
-
-
8-amino-7-oxononanoate synthase
-
8-amino-7-oxononanoate synthase
-
-
8-amino-7-oxononanoate synthase
Geobacillus kaustophilus JCM12893
-
-
-
8-amino-7-oxononanoate synthase
-
-
8-amino-7-oxononanoate synthase
Ruminiclostridium thermocellum ATCC27405
-
-
-
8-amino-7-oxononanoate synthase
-
-
8-amino-7-oxononanoate synthase
Symbiobacterium thermophilum IAM14863
-
-
-
8-amino-7-oxononanoate synthase
-
-
8-amino-7-oxopelargonate synthase
-
-
-
-
bioF protein
-
-
bioF protein
Escherichia coli C268
-
-
-
DAPA AT
-
-
DAPA AT
Escherichia coli C268
-
-
-
synthase, 7-oxo-8-aminononanoate
-
-
-
-
synthetase, 7-keto-8-aminopelargonate
-
-
-
-
KAPA synthetase
-
-
additional information
-
the enzyme is a member of the alpha-oxoamine synthase enzyme family
additional information
-
the enzyme belongs to subclass II of the aminotransferase family
CAS REGISTRY NUMBER
COMMENTARY
9075-61-0
-
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
ecotype Wassilewskija
SwissProt
Manually annotated by BRENDA team
Erwinia aroidea
-
-
-
Manually annotated by BRENDA team
biotin-auxotroph mutants, derived from K-12 parent strain Y10-1
-
-
Manually annotated by BRENDA team
Escherichia coli C268
C268
-
-
Manually annotated by BRENDA team
Geobacillus kaustophilus JCM12893
-
-
-
Manually annotated by BRENDA team
strain IFO 3525
-
-
Manually annotated by BRENDA team
Lysinibacillus sphaericus IFO 3525
strain IFO 3525
-
-
Manually annotated by BRENDA team
Ruminiclostridium thermocellum ATCC27405
-
-
-
Manually annotated by BRENDA team
Sporobolomyces coprophilus
-
-
-
Manually annotated by BRENDA team
Symbiobacterium thermophilum IAM14863
-
-
-
Manually annotated by BRENDA team
SUBSTRATE
PRODUCT                      
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
(R)-8-amino-7-oxononanoic acid + S-adenosyl-L-methionine
(7R,8S)-diaminopelargonic acid + S-adenosyl-(4-methylthio-2-oxobutanoic acid)
show the reaction diagram
-
8.6% product is formed matching the portion of S-enantiomer substrate (9.3%),37C, direct assay with 100 mM N-(2-hydroxyethyl)piperazine-N'-(2-propanesulfonic acid) buffer (pH 8.6), 0.1 mM pyridoxal 5'-phosphate, 1 mM S-adenosyl-L-methionine, 10 microM (R)-8-amino-7-oxononanoic acid
-
?
(S)-8-amino-7-oxononanoic acid + (R)-8-amino-7-oxononanoic acid + S-adenosyl-L-methionine
(7R,8S)-diaminopelargonic acid + S-adenosyl-(4-methylthio-2-oxobutanoic acid)
show the reaction diagram
-
46.3% product is formed from the racemic substrate, 37C, direct assay with 100 mM N-(2-hydroxyethyl)piperazine-N'-(2-propanesulfonic acid) buffer (pH 8.6), 0.1 mM pyridoxal 5'-phosphate, 1 mM S-adenosyl-L-methionine, 2 microM racemic 8-amino-7-oxononanoic acid
-
?
(S)-8-amino-7-oxononanoic acid + S-adenosyl-L-methionine
(7R,8S)-diaminopelargonic acid + S-adenosyl-(4-methylthio-2-oxobutanoic acid)
show the reaction diagram
-
37C, direct assay with 100 mM N-(2-hydroxyethyl)piperazine-N'-(2-propanesulfonic acid) buffer (pH 8.6), 0.1 mM pyridoxal 5'-phosphate, 1 mM S-adenosyl-L-methionine, 2 microM (S)-8-amino-7-oxononanoic acid
-
?
(S)-8-amino-7-oxononanoic acid + S-adenosyl-L-methionine
(7R,8S)-diaminopelargonic acid + S-adenosyl-(4-methylthio-2-oxobutanoic acid)
show the reaction diagram
-
37C, direct assay with 100 mM N-(2-hydroxyethyl)piperazine-N'-(2-propanesulfonic acid) buffer (pH 8.6), 0.1 mM pyridoxal 5'-phosphate, varying S-adenosyl-L-methionine, 9 microM (S)-8-amino-7-oxononanoic acid, varying inhibitor concentration
-
?
(S)-8-amino-7-oxononanoic acid + S-adenosyl-L-methionine
(7R,8S)-diaminopelargonic acid + S-adenosyl-(4-methylthio-2-oxobutanoic acid)
show the reaction diagram
-
93.2% product is formed matching the portion of S-enantiomer substrate (94.6%), 37C, direct assay with 100 mM N-(2-hydroxyethyl)piperazine-N'-(2-propanesulfonic acid) buffer (pH 8.6), 0.1 mM pyridoxal 5'-phosphate, 1 mM S-adenosyl-L-methionine, 2 microM (S)-8-amino-7-oxononanoic acid
-
?
(S)-8-amino-7-oxononanoic acid + S-adenosyl-L-methionine
(7R,8S)-diaminopelargonic acid + S-adenosyl-(4-methylthio-2-oxobutanoic acid)
show the reaction diagram
Escherichia coli C268
-
37C, direct assay with 100 mM N-(2-hydroxyethyl)piperazine-N'-(2-propanesulfonic acid) buffer (pH 8.6), 0.1 mM pyridoxal 5'-phosphate, varying S-adenosyl-L-methionine, 9 microM (S)-8-amino-7-oxononanoic acid, varying inhibitor concentration
-
?
6-carboxyhexanoyl-CoA + D-alanine
8-amino-7-oxononanoate + CoA + CO2
show the reaction diagram
-
the L-isomer of the amino acid is preferred, D-alanine shows 5fold slower reaction, interaction analysis, overview
i.e. D-KAPA
?
6-carboxyhexanoyl-CoA + L-alanine
8-amino-7-oxononanoate + CoA + CO2
show the reaction diagram
-
-
-
?
6-carboxyhexanoyl-CoA + L-alanine
8-amino-7-oxononanoate + CoA + CO2
show the reaction diagram
-
absolutely specific for L-alanine
i.e. 7-oxo-8-amino-pelargonic acid
?
6-carboxyhexanoyl-CoA + L-alanine
8-amino-7-oxononanoate + CoA + CO2
show the reaction diagram
-
i.e. pimeloyl-CoA
i.e. 7-oxo-8-amino-pelargonic acid
?
6-carboxyhexanoyl-CoA + L-alanine
8-amino-7-oxononanoate + CoA + CO2
show the reaction diagram
-
i.e. pimeloyl-CoA
i.e. 7-oxo-8-amino-pelargonic acid
?
6-carboxyhexanoyl-CoA + L-alanine
8-amino-7-oxononanoate + CoA + CO2
show the reaction diagram
-
i.e. pimeloyl-CoA
i.e. 7-oxo-8-amino-pelargonic acid
?
6-carboxyhexanoyl-CoA + L-alanine
8-amino-7-oxononanoate + CoA + CO2
show the reaction diagram
-
i.e. pimeloyl-CoA
i.e. 7-oxo-8-amino-pelargonic acid
?
6-carboxyhexanoyl-CoA + L-alanine
8-amino-7-oxononanoate + CoA + CO2
show the reaction diagram
i.e. pimeloyl-CoA
i.e. 7-oxo-8-amino-pelargonic acid
?
6-carboxyhexanoyl-CoA + L-alanine
8-amino-7-oxononanoate + CoA + CO2
show the reaction diagram
-
i.e. pimeloyl-CoA
i.e. 7-oxo-8-amino-pelargonic acid
ir
6-carboxyhexanoyl-CoA + L-alanine
8-amino-7-oxononanoate + CoA + CO2
show the reaction diagram
-
i.e. pimeloyl-CoA
i.e. 7-oxo-8-amino-pelargonic acid
ir
6-carboxyhexanoyl-CoA + L-alanine
8-amino-7-oxononanoate + CoA + CO2
show the reaction diagram
-
i.e. pimeloyl-CoA
i.e. 7-oxo-8-amino-pelargonic acid
?
6-carboxyhexanoyl-CoA + L-alanine
8-amino-7-oxononanoate + CoA + CO2
show the reaction diagram
-
i.e. pimeloyl-CoA
i.e. 7-oxo-8-amino-pelargonic acid
?
6-carboxyhexanoyl-CoA + L-alanine
8-amino-7-oxononanoate + CoA + CO2
show the reaction diagram
-
i.e. pimeloyl-CoA
i.e. 7-oxo-8-amino-pelargonic acid
?
6-carboxyhexanoyl-CoA + L-alanine
8-amino-7-oxononanoate + CoA + CO2
show the reaction diagram
-
i.e. pimeloyl-CoA
i.e. 7-oxo-8-amino-pelargonic acid
?
6-carboxyhexanoyl-CoA + L-alanine
8-amino-7-oxononanoate + CoA + CO2
show the reaction diagram
-
i.e. pimeloyl-CoA
i.e. 7-oxo-8-amino-pelargonic acid
?
6-carboxyhexanoyl-CoA + L-alanine
8-amino-7-oxononanoate + CoA + CO2
show the reaction diagram
-
i.e. pimeloyl-CoA
i.e. 7-oxo-8-amino-pelargonic acid
ir
6-carboxyhexanoyl-CoA + L-alanine
8-amino-7-oxononanoate + CoA + CO2
show the reaction diagram
-
i.e. pimeloyl-CoA
i.e. 7-oxo-8-amino-pelargonic acid
ir
6-carboxyhexanoyl-CoA + L-alanine
8-amino-7-oxononanoate + CoA + CO2
show the reaction diagram
-
i.e. pimeloyl-CoA
i.e. 7-oxo-8-amino-pelargonic acid
ir
6-carboxyhexanoyl-CoA + L-alanine
8-amino-7-oxononanoate + CoA + CO2
show the reaction diagram
-
i.e. pimeloyl-CoA
i.e. 7-oxo-8-amino-pelargonic acid
?
6-carboxyhexanoyl-CoA + L-alanine
8-amino-7-oxononanoate + CoA + CO2
show the reaction diagram
Lipomyces starkeyi, Sporidiobolus salmonicolor, Sporobolomyces coprophilus
-
i.e. pimeloyl-CoA
i.e. 7-oxo-8-amino-pelargonic acid
?
6-carboxyhexanoyl-CoA + L-alanine
8-amino-7-oxononanoate + CoA + CO2
show the reaction diagram
Citrobacter freundii, Erwinia aroidea
-
i.e. pimeloyl-CoA
i.e. 7-oxo-8-amino-pelargonic acid
?
6-carboxyhexanoyl-CoA + L-alanine
8-amino-7-oxononanoate + CoA + CO2
show the reaction diagram
-
L-cysteine cannot replace L-alanine
i.e. 7-oxo-8-amino-pelargonic acid
?
6-carboxyhexanoyl-CoA + L-alanine
8-amino-7-oxononanoate + CoA + CO2
show the reaction diagram
-
second step in biotin biosynthesis
i.e. 7-oxo-8-amino-pelargonic acid
ir
6-carboxyhexanoyl-CoA + L-alanine
8-amino-7-oxononanoate + CoA + CO2
show the reaction diagram
-
second step in biotin biosynthesis
i.e. 7-oxo-8-amino-pelargonic acid
ir
6-carboxyhexanoyl-CoA + L-alanine
8-amino-7-oxononanoate + CoA + CO2
show the reaction diagram
-
reaction in biotin biosynthesis
i.e. 7-oxo-8-amino-pelargonic acid
?
6-carboxyhexanoyl-CoA + L-alanine
8-amino-7-oxononanoate + CoA + CO2
show the reaction diagram
-
reaction in biotin biosynthesis
i.e. 7-oxo-8-amino-pelargonic acid
?
6-carboxyhexanoyl-CoA + L-alanine
8-amino-7-oxononanoate + CoA + CO2
show the reaction diagram
-
reaction in biotin biosynthesis
i.e. 7-oxo-8-amino-pelargonic acid
?
6-carboxyhexanoyl-CoA + L-alanine
8-amino-7-oxononanoate + CoA + CO2
show the reaction diagram
-
reaction in biotin biosynthesis
i.e. 7-oxo-8-amino-pelargonic acid
?
6-carboxyhexanoyl-CoA + L-alanine
8-amino-7-oxononanoate + CoA + CO2
show the reaction diagram
reaction in biotin biosynthesis
i.e. 7-oxo-8-amino-pelargonic acid
?
6-carboxyhexanoyl-CoA + L-alanine
8-amino-7-oxononanoate + CoA + CO2
show the reaction diagram
-
reaction in biotin biosynthesis
i.e. 7-oxo-8-amino-pelargonic acid
ir
6-carboxyhexanoyl-CoA + L-alanine
8-amino-7-oxononanoate + CoA + CO2
show the reaction diagram
-
reaction in biotin biosynthesis
i.e. 7-oxo-8-amino-pelargonic acid
ir
6-carboxyhexanoyl-CoA + L-alanine
8-amino-7-oxononanoate + CoA + CO2
show the reaction diagram
-
reaction in biotin biosynthesis
i.e. 7-oxo-8-amino-pelargonic acid
?
6-carboxyhexanoyl-CoA + L-alanine
8-amino-7-oxononanoate + CoA + CO2
show the reaction diagram
-
reaction in biotin biosynthesis
i.e. 7-oxo-8-amino-pelargonic acid
?
6-carboxyhexanoyl-CoA + L-alanine
8-amino-7-oxononanoate + CoA + CO2
show the reaction diagram
-
reaction in biotin biosynthesis
i.e. 7-oxo-8-amino-pelargonic acid
?
6-carboxyhexanoyl-CoA + L-alanine
8-amino-7-oxononanoate + CoA + CO2
show the reaction diagram
-
reaction in biotin biosynthesis
i.e. 7-oxo-8-amino-pelargonic acid
?
6-carboxyhexanoyl-CoA + L-alanine
8-amino-7-oxononanoate + CoA + CO2
show the reaction diagram
-
reaction in biotin biosynthesis
i.e. 7-oxo-8-amino-pelargonic acid
?
6-carboxyhexanoyl-CoA + L-alanine
8-amino-7-oxononanoate + CoA + CO2
show the reaction diagram
-
reaction in biotin biosynthesis
i.e. 7-oxo-8-amino-pelargonic acid
ir
6-carboxyhexanoyl-CoA + L-alanine
8-amino-7-oxononanoate + CoA + CO2
show the reaction diagram
-
reaction in biotin biosynthesis
i.e. 7-oxo-8-amino-pelargonic acid
ir
6-carboxyhexanoyl-CoA + L-alanine
8-amino-7-oxononanoate + CoA + CO2
show the reaction diagram
-
reaction in biotin biosynthesis
i.e. 7-oxo-8-amino-pelargonic acid
ir
6-carboxyhexanoyl-CoA + L-alanine
8-amino-7-oxononanoate + CoA + CO2
show the reaction diagram
-
reaction in biotin biosynthesis
i.e. 7-oxo-8-amino-pelargonic acid
?
6-carboxyhexanoyl-CoA + L-alanine
8-amino-7-oxononanoate + CoA + CO2
show the reaction diagram
Lipomyces starkeyi, Sporidiobolus salmonicolor, Sporobolomyces coprophilus
-
reaction in biotin biosynthesis
i.e. 7-oxo-8-amino-pelargonic acid
?
6-carboxyhexanoyl-CoA + L-alanine
8-amino-7-oxononanoate + CoA + CO2
show the reaction diagram
Citrobacter freundii, Erwinia aroidea
-
reaction in biotin biosynthesis
i.e. 7-oxo-8-amino-pelargonic acid
?
6-carboxyhexanoyl-CoA + L-alanine
8-amino-7-oxononanoate + CoA + CO2
show the reaction diagram
-
first committed step in the biotin biosynthesis pathway
-
?
6-carboxyhexanoyl-CoA + L-alanine
8-amino-7-oxononanoate + CoA + CO2
show the reaction diagram
-
the enzyme catalyzes the first committed step in the four step pathway, the decarboxylative condensation of L-alanine and pimeloyl-CoA to give (7S)-8-amino-7-oxononanoate, a Claisen condensation
-
?
6-carboxyhexanoyl-CoA + L-alanine
8-amino-7-oxononanoate + CoA + CO2
show the reaction diagram
-
the L-isomer of the amino acid is preferred giving a 5fold faster reaction, interaction analysis, overview
i.e. L-KAPA
?
6-carboxyhexanoyl-CoA + L-alanine
8-amino-7-oxononanoate + CoA + CO2
show the reaction diagram
Lysinibacillus sphaericus IFO 3525
-
i.e. pimeloyl-CoA
i.e. 7-oxo-8-amino-pelargonic acid
?
6-carboxyhexanoyl-CoA + L-serine
9-hydroxy-8-amino-7-oxononanoate + CoA
show the reaction diagram
-
low activity
-
?
glycine + acetyl-CoA
?
show the reaction diagram
Symbiobacterium thermophilum, Symbiobacterium thermophilum IAM14863
-
-
-
-
?
glycine + pimeloyl-CoA
?
show the reaction diagram
Symbiobacterium thermophilum, Symbiobacterium thermophilum IAM14863
-
-
-
-
?
L-alanine + acetyl-CoA
?
show the reaction diagram
Symbiobacterium thermophilum, Symbiobacterium thermophilum IAM14863
-
-
-
-
?
L-alanine + pimeloyl-CoA
8-amino-7-oxononanoate + CoA + CO2
show the reaction diagram
-
-
-
?
L-alanine + pimeloyl-CoA
8-amino-7-oxononanoate + CoA + CO2
show the reaction diagram
-
-
-
?
L-alanine + pimeloyl-CoA
8-amino-7-oxononanoate + CoA + CO2
show the reaction diagram
-
-
-
?
L-alanine + pimeloyl-CoA
8-amino-7-oxononanoate + CoA + CO2
show the reaction diagram
-
-
-
?
L-alanine + pimeloyl-CoA
8-amino-7-oxononanoate + CoA + CO2
show the reaction diagram
-
-
-
?
L-alanine + pimeloyl-CoA
8-amino-7-oxononanoate + CoA + CO2
show the reaction diagram
-
no activity observed with acetyl-CoA, no activity observed with glycine or L-serine
-
?
L-alanine + pimeloyl-CoA
8-amino-7-oxononanoate + CoA + CO2
show the reaction diagram
-
no activity observed with L-serine
-
?
L-alanine + pimeloyl-CoA
8-amino-7-oxononanoate + CoA + CO2
show the reaction diagram
Geobacillus kaustophilus JCM12893
-
no activity observed with acetyl-CoA, no activity observed with glycine or L-serine
-
?
L-alanine + pimeloyl-CoA
8-amino-7-oxononanoate + CoA + CO2
show the reaction diagram
Symbiobacterium thermophilum IAM14863
-
no activity observed with L-serine
-
?
pimeloyl-CoA + D-alanine
?
show the reaction diagram
-
-
-
-
?
pimeloyl-CoA + L-alanine
8-amino-7-oxononanoate + CoA + CO2
show the reaction diagram
the enzyme is strictly stereospecific for L-alanine
-
?
pimeloyl-CoA + L-alanine
?
show the reaction diagram
-
-
-
-
?
pimeloyl-CoA + L-alanine methyl ester
?
show the reaction diagram
-
trapping and determination of the reaction intermediate using the the more stable methyl ester of the substrate, overview
-
-
?
L-alanine + pimeloyl-CoA
8-amino-7-oxononanoate + CoA + CO2
show the reaction diagram
Ruminiclostridium thermocellum ATCC27405
-
-
-
?
additional information
?
-
the enzyme catalyzes the first committed enzyme of the biotin synthesis pathway
-
-
-
additional information
?
-
-
pimeloyl-CoA forms a quinonoid with L- or D-KAPA
-
-
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
(S)-8-amino-7-oxononanoic acid + S-adenosyl-L-methionine
(7R,8S)-diaminopelargonic acid + S-adenosyl-(4-methylthio-2-oxobutanoic acid)
show the reaction diagram
-
37C, direct assay with 100 mM N-(2-hydroxyethyl)piperazine-N'-(2-propanesulfonic acid) buffer (pH 8.6), 0.1 mM pyridoxal 5'-phosphate, 1 mM S-adenosyl-L-methionine, 2 microM (S)-8-amino-7-oxononanoic acid
-
?
(S)-8-amino-7-oxononanoic acid + S-adenosyl-L-methionine
(7R,8S)-diaminopelargonic acid + S-adenosyl-(4-methylthio-2-oxobutanoic acid)
show the reaction diagram
Escherichia coli, Escherichia coli C268
-
37C, direct assay with 100 mM N-(2-hydroxyethyl)piperazine-N'-(2-propanesulfonic acid) buffer (pH 8.6), 0.1 mM pyridoxal 5'-phosphate, varying S-adenosyl-L-methionine, 9 microM (S)-8-amino-7-oxononanoic acid, varying inhibitor concentration
-
?
6-carboxyhexanoyl-CoA + L-alanine
8-amino-7-oxononanoate + CoA + CO2
show the reaction diagram
-
-
-
?
6-carboxyhexanoyl-CoA + L-alanine
8-amino-7-oxononanoate + CoA + CO2
show the reaction diagram
-
i.e. pimeloyl-CoA
i.e. 7-oxo-8-amino-pelargonic acid
?
6-carboxyhexanoyl-CoA + L-alanine
8-amino-7-oxononanoate + CoA + CO2
show the reaction diagram
-
i.e. pimeloyl-CoA
i.e. 7-oxo-8-amino-pelargonic acid
?
6-carboxyhexanoyl-CoA + L-alanine
8-amino-7-oxononanoate + CoA + CO2
show the reaction diagram
-
i.e. pimeloyl-CoA
i.e. 7-oxo-8-amino-pelargonic acid
?
6-carboxyhexanoyl-CoA + L-alanine
8-amino-7-oxononanoate + CoA + CO2
show the reaction diagram
-
i.e. pimeloyl-CoA
i.e. 7-oxo-8-amino-pelargonic acid
?
6-carboxyhexanoyl-CoA + L-alanine
8-amino-7-oxononanoate + CoA + CO2
show the reaction diagram
P12998
i.e. pimeloyl-CoA
i.e. 7-oxo-8-amino-pelargonic acid
?
6-carboxyhexanoyl-CoA + L-alanine
8-amino-7-oxononanoate + CoA + CO2
show the reaction diagram
-
i.e. pimeloyl-CoA
i.e. 7-oxo-8-amino-pelargonic acid
ir
6-carboxyhexanoyl-CoA + L-alanine
8-amino-7-oxononanoate + CoA + CO2
show the reaction diagram
-
i.e. pimeloyl-CoA
i.e. 7-oxo-8-amino-pelargonic acid
ir
6-carboxyhexanoyl-CoA + L-alanine
8-amino-7-oxononanoate + CoA + CO2
show the reaction diagram
-
i.e. pimeloyl-CoA
i.e. 7-oxo-8-amino-pelargonic acid
?
6-carboxyhexanoyl-CoA + L-alanine
8-amino-7-oxononanoate + CoA + CO2
show the reaction diagram
-
i.e. pimeloyl-CoA
i.e. 7-oxo-8-amino-pelargonic acid
?
6-carboxyhexanoyl-CoA + L-alanine
8-amino-7-oxononanoate + CoA + CO2
show the reaction diagram
-
i.e. pimeloyl-CoA
i.e. 7-oxo-8-amino-pelargonic acid
?
6-carboxyhexanoyl-CoA + L-alanine
8-amino-7-oxononanoate + CoA + CO2
show the reaction diagram
-
i.e. pimeloyl-CoA
i.e. 7-oxo-8-amino-pelargonic acid
?
6-carboxyhexanoyl-CoA + L-alanine
8-amino-7-oxononanoate + CoA + CO2
show the reaction diagram
-
i.e. pimeloyl-CoA
i.e. 7-oxo-8-amino-pelargonic acid
?
6-carboxyhexanoyl-CoA + L-alanine
8-amino-7-oxononanoate + CoA + CO2
show the reaction diagram
-
i.e. pimeloyl-CoA
i.e. 7-oxo-8-amino-pelargonic acid
ir
6-carboxyhexanoyl-CoA + L-alanine
8-amino-7-oxononanoate + CoA + CO2
show the reaction diagram
-
i.e. pimeloyl-CoA
i.e. 7-oxo-8-amino-pelargonic acid
ir
6-carboxyhexanoyl-CoA + L-alanine
8-amino-7-oxononanoate + CoA + CO2
show the reaction diagram
-
i.e. pimeloyl-CoA
i.e. 7-oxo-8-amino-pelargonic acid
ir
6-carboxyhexanoyl-CoA + L-alanine
8-amino-7-oxononanoate + CoA + CO2
show the reaction diagram
-
i.e. pimeloyl-CoA
i.e. 7-oxo-8-amino-pelargonic acid
?
6-carboxyhexanoyl-CoA + L-alanine
8-amino-7-oxononanoate + CoA + CO2
show the reaction diagram
Lipomyces starkeyi, Sporidiobolus salmonicolor, Sporobolomyces coprophilus
-
i.e. pimeloyl-CoA
i.e. 7-oxo-8-amino-pelargonic acid
?
6-carboxyhexanoyl-CoA + L-alanine
8-amino-7-oxononanoate + CoA + CO2
show the reaction diagram
Citrobacter freundii, Erwinia aroidea
-
i.e. pimeloyl-CoA
i.e. 7-oxo-8-amino-pelargonic acid
?
6-carboxyhexanoyl-CoA + L-alanine
8-amino-7-oxononanoate + CoA + CO2
show the reaction diagram
-
second step in biotin biosynthesis
i.e. 7-oxo-8-amino-pelargonic acid
ir
6-carboxyhexanoyl-CoA + L-alanine
8-amino-7-oxononanoate + CoA + CO2
show the reaction diagram
-
second step in biotin biosynthesis
i.e. 7-oxo-8-amino-pelargonic acid
ir
6-carboxyhexanoyl-CoA + L-alanine
8-amino-7-oxononanoate + CoA + CO2
show the reaction diagram
-
reaction in biotin biosynthesis
i.e. 7-oxo-8-amino-pelargonic acid
?
6-carboxyhexanoyl-CoA + L-alanine
8-amino-7-oxononanoate + CoA + CO2
show the reaction diagram
-
reaction in biotin biosynthesis
i.e. 7-oxo-8-amino-pelargonic acid
?
6-carboxyhexanoyl-CoA + L-alanine
8-amino-7-oxononanoate + CoA + CO2
show the reaction diagram
-
reaction in biotin biosynthesis
i.e. 7-oxo-8-amino-pelargonic acid
?
6-carboxyhexanoyl-CoA + L-alanine
8-amino-7-oxononanoate + CoA + CO2
show the reaction diagram
-
reaction in biotin biosynthesis
i.e. 7-oxo-8-amino-pelargonic acid
?
6-carboxyhexanoyl-CoA + L-alanine
8-amino-7-oxononanoate + CoA + CO2
show the reaction diagram
P12998
reaction in biotin biosynthesis
i.e. 7-oxo-8-amino-pelargonic acid
?
6-carboxyhexanoyl-CoA + L-alanine
8-amino-7-oxononanoate + CoA + CO2
show the reaction diagram
-
reaction in biotin biosynthesis
i.e. 7-oxo-8-amino-pelargonic acid
ir
6-carboxyhexanoyl-CoA + L-alanine
8-amino-7-oxononanoate + CoA + CO2
show the reaction diagram
-
reaction in biotin biosynthesis
i.e. 7-oxo-8-amino-pelargonic acid
ir
6-carboxyhexanoyl-CoA + L-alanine
8-amino-7-oxononanoate + CoA + CO2
show the reaction diagram
-
reaction in biotin biosynthesis
i.e. 7-oxo-8-amino-pelargonic acid
?
6-carboxyhexanoyl-CoA + L-alanine
8-amino-7-oxononanoate + CoA + CO2
show the reaction diagram
-
reaction in biotin biosynthesis
i.e. 7-oxo-8-amino-pelargonic acid
?
6-carboxyhexanoyl-CoA + L-alanine
8-amino-7-oxononanoate + CoA + CO2
show the reaction diagram
-
reaction in biotin biosynthesis
i.e. 7-oxo-8-amino-pelargonic acid
?
6-carboxyhexanoyl-CoA + L-alanine
8-amino-7-oxononanoate + CoA + CO2
show the reaction diagram
-
reaction in biotin biosynthesis
i.e. 7-oxo-8-amino-pelargonic acid
?
6-carboxyhexanoyl-CoA + L-alanine
8-amino-7-oxononanoate + CoA + CO2
show the reaction diagram
-
reaction in biotin biosynthesis
i.e. 7-oxo-8-amino-pelargonic acid
?
6-carboxyhexanoyl-CoA + L-alanine
8-amino-7-oxononanoate + CoA + CO2
show the reaction diagram
-
reaction in biotin biosynthesis
i.e. 7-oxo-8-amino-pelargonic acid
ir
6-carboxyhexanoyl-CoA + L-alanine
8-amino-7-oxononanoate + CoA + CO2
show the reaction diagram
-
reaction in biotin biosynthesis
i.e. 7-oxo-8-amino-pelargonic acid
ir
6-carboxyhexanoyl-CoA + L-alanine
8-amino-7-oxononanoate + CoA + CO2
show the reaction diagram
-
reaction in biotin biosynthesis
i.e. 7-oxo-8-amino-pelargonic acid
ir
6-carboxyhexanoyl-CoA + L-alanine
8-amino-7-oxononanoate + CoA + CO2
show the reaction diagram
-
reaction in biotin biosynthesis
i.e. 7-oxo-8-amino-pelargonic acid
?
6-carboxyhexanoyl-CoA + L-alanine
8-amino-7-oxononanoate + CoA + CO2
show the reaction diagram
Lipomyces starkeyi, Sporidiobolus salmonicolor, Sporobolomyces coprophilus
-
reaction in biotin biosynthesis
i.e. 7-oxo-8-amino-pelargonic acid
?
6-carboxyhexanoyl-CoA + L-alanine
8-amino-7-oxononanoate + CoA + CO2
show the reaction diagram
Citrobacter freundii, Erwinia aroidea
-
reaction in biotin biosynthesis
i.e. 7-oxo-8-amino-pelargonic acid
?
6-carboxyhexanoyl-CoA + L-alanine
8-amino-7-oxononanoate + CoA + CO2
show the reaction diagram
-
first committed step in the biotin biosynthesis pathway
-
?
6-carboxyhexanoyl-CoA + L-alanine
8-amino-7-oxononanoate + CoA + CO2
show the reaction diagram
-
the enzyme catalyzes the first committed step in the four step pathway, the decarboxylative condensation of L-alanine and pimeloyl-CoA to give (7S)-8-amino-7-oxononanoate
-
?
pimeloyl-CoA + L-alanine
8-amino-7-oxononanoate + CoA + CO2
show the reaction diagram
Q8GW43
-
-
?
6-carboxyhexanoyl-CoA + L-alanine
8-amino-7-oxononanoate + CoA + CO2
show the reaction diagram
Lysinibacillus sphaericus IFO 3525
-
i.e. pimeloyl-CoA
i.e. 7-oxo-8-amino-pelargonic acid
?
additional information
?
-
Q8GW43
the enzyme catalyzes the first committed enzyme of the biotin synthesis pathway
-
-
-
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
pyridoxal 5'-phosphate
-
dependent on
pyridoxal 5'-phosphate
-
-
pyridoxal 5'-phosphate
-
requirement, pyridoxal-5'-phosphate protein, not replaceable by pyridoxal, pyridoxine, pyridoxine 5-phosphate, pyridoxamine, pyridoxamine 5-phosphate
pyridoxal 5'-phosphate
-
dependent on; incubation of enzyme with L-alanine but without pyridoxal-5'-phosphate lead to abortive transamination
pyridoxal 5'-phosphate
-
Schiff base formation between D- or L-alanine and pyridoxal-5'-phophate in the active site
pyridoxal 5'-phosphate
-
-
pyridoxal 5'-phosphate
-
pyridoxal-5'-phosphate binding site
pyridoxal 5'-phosphate
-
dependent on
pyridoxal 5'-phosphate
-
dependent on
pyridoxal 5'-phosphate
-
dependent on, binding structure
pyridoxal 5'-phosphate
dependent on
pyridoxal 5'-phosphate
-
-
pyridoxal 5'-phosphate
-
-
pyridoxal 5'-phosphate
-
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
-
effects of several metal ions on biotin biosynthesis
additional information
-
no metal ion requirement
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
(R)-8-amino-7-oxononanoic acid
-
no inhibition up to 15 microM with 94.6% ee (S)-enantiomer as substrate, beyond that strong inhibitor of both enzyme forms, binding to active site
1,10-phenanthroline
-
to some extent
2,3-dichloronaphthalene-1,4-dione
-
-
2-(furan-2-yl)-1H-benzimidazole
-
-
2-amino-3-hydroxy-2-methylnonadioic acid
-
competitive, transition state analogue
2-[(1,1,2,2-tetrachloroethyl)sulfanyl]-3a,4,7,7a-tetrahydro-1H-isoindole-1,3(2H)-dione
-
-
2-[(trichloromethyl)sulfanyl]-3a,4,7,7a-tetrahydro-1H-isoindole-1,3(2H)-dione
-
-
4-(1H-inden-3-yl)naphthalene-1,2-dione
-
-
4-carboxybutyl(1-amino-1-carboxyethyl)phosphonate
-
competitive, transition state analogue
5,10-dioxo-5,10-dihydronaphtho[2,3-b][1,4]dithiine-2,3-dicarbonitrile
-
-
5,8-dihydronaphthalene-1,4-dione
-
-
5,8-dihydroxynaphthalene-1,4-dione
-
-
5-hydroxy-2-methylnaphthalene-1,4-dione
-
-
5-hydroxynaphthalene-1,4-dione
-
-
8-amino-7-oxo-8-phosphonononanoic acid
-
strong inhibition
8-Amino-7-oxononanoate
-
product inhibition in vivo
8-amino-7-oxooctanoic acid
-
achiral analog of substrate, strong inhibitor of both enzyme forms, binding to active site
citrate
-
to some extent
D-alanine
-
competitive; Schiff base formation between D- or L-alanine and pyridoxal-5'-phophate in the active site
D-cycloserine
-
-
D-KAPA
-
product inhibition
D-penicillamine
-
L-enantiomer not as effective
diisopropyl fluorophosphate
-
to some extent
hydroxylamine
-
-
isoniazide
-
to some extent
L-cysteine
-
strong
methyl 3-(5,6-dioxo-5,6-dihydronaphthalen-2-yl)propanoate
-
-
methyl 3-[8-(1H-inden-3-yl)-5,6-dioxo-5,6-dihydronaphthalen-2-yl]propanoate
-
-
methyl 3-[8-[(4-fluorophenyl)amino]-5,6-dioxo-5,6-dihydronaphthalen-2-yl]propanoate
-
-
N-[dichloro(fluoro)-l4-sulfanyl]-N',N'-dimethyl-N-phenylsulfuric diamide
-
-
N-[dichloro(fluoromethyl)-lambda4-sulfanyl]-N',N'-dimethyl-N-(4-methylphenyl)sulfuric diamide
-
-
naphthalene-1,2-dione
-
-
phenylhydrazine
-
-
pyridoxal 5'-phosphate
-
high concentrations
Pyruvic acid
-
-
Semicarbazide
-
-
trifluoroalanine
-
binding structure, irreversible suicide inhibition of the enzyme, involves decarboxylative defluorination of the inhibitor-PLP aldimine followed by attack of the conjugated imine by the amino group of the active site lysine to afford a covalently bound difluorinated intermediate, which can subsequently undergo further HF losses and hydrolysis to afford a 2-(pyridoximine phosphate) acetoyl protein adduct
triphenyltin acetate
-
herbicidal activity (foliar treatment) under greenhouse conditions
-
methyl 3-[8-[(4-methylphenyl)amino]-5,6-dioxo-5,6-dihydronaphthalen-2-yl]propanoate
-
-
additional information
-
no inhibition by HgCl2, EDTA, 2,2'-dipyridyl, oxalate, KCN, various amino acids
-
additional information
-
inhibition mechanism; no inhibition by 8-amino-7-oxo-8-phosphonononanoic acid
-
additional information
-
concentration above 10 mM of Ca2+, Mg2+, and Mn2+ cause slow precipitation of the enzyme
-
additional information
-
no inhibition by D-alanine
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0013
(S)-8-amino-7-oxononanoic acid
-
calculated from the competitive and uncompetitive constants and the substrate concentration determined in inhibitor experiments, 37C, pH 8.6
0.2015
D-alanine
-
pH 7.7, 25C, recombinant enzyme, with pimeloyl-CoA
0.002
L-alanine
-
-
0.09
L-alanine
-
pH 6.0, 60C
0.23
L-alanine
-
pH 6.0, 60C
0.25
L-alanine
-
5-aminolevulinate synthase-fusion protein (single chain chimeric dimer), pH 7.5, 30C
0.4675
L-alanine
-
pH 7.7, 25C, recombinant enzyme, with pimeloyl-CoA
0.5
L-alanine
-
-
0.5
L-alanine
-
wild type protein, pH not specified in the publication, temperature not specified in the publication
0.5
L-alanine
-
pH not specified in the publication, temperature not specified in the publication
0.9
L-alanine
-
-
1.4
L-alanine
pH 7.5, 30C, recombinant enzyme
2.28
L-alanine
-
pH 6.0, 60C
0.001
pimeloyl-CoA
-
-
0.0015
pimeloyl-CoA
-
-
0.0015
pimeloyl-CoA
-
pH 7.7, 25C, recombinant enzyme
0.0016
pimeloyl-CoA
pH 7.5, 30C, recombinant enzyme
0.01
pimeloyl-CoA
-
5-aminolevulinate synthase-fusion protein (single chain chimeric dimer), pH 7.5, 30C
0.01
pimeloyl-CoA
-
pH 6.0, 60C
0.02
pimeloyl-CoA
-
pH 6.0, 60C
0.025
pimeloyl-CoA
-
-
0.025
pimeloyl-CoA
-
wild type protein, pH not specified in the publication, temperature not specified in the publication
0.025
pimeloyl-CoA
-
pH not specified in the publication, temperature not specified in the publication
0.03
pimeloyl-CoA
-
pH 6.0, 60C
0.07
pimeloyl-CoA
-
-
0.0014
S-adenosyl-L-methionine
-
calculated from the competitive and uncompetitive constants and the substrate concentration determined in inhibitor experiments, 37C, pH 8.6
additional information
additional information
-
stopped-flow kinetics of enzyme interaction with L-alanine and D-alanine, steady-state kinetics and thermodynamics
-
additional information
additional information
the recombinant KAPA synthase obeys Michaelis-Menten kinetics with respect to pimeloyl-CoA and L-Ala
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0036
D-alanine
Mycobacterium tuberculosis
-
pH 7.7, 25C, recombinant enzyme, with pimeloyl-CoA
0.007
L-alanine
Mycobacterium tuberculosis
-
pH 7.7, 25C, recombinant enzyme, with pimeloyl-CoA
0.028
L-alanine
Escherichia coli
-
5-aminolevulinate synthase-fusion protein (single chain chimeric dimer), pH 7.5, 30C
0.06
L-alanine
Escherichia coli
-
wild type protein, pH not specified in the publication, temperature not specified in the publication
0.11
L-alanine
Arabidopsis thaliana
Q8GW43
pH 7.5, 30C, recombinant enzyme
0.000833
pimeloyl-CoA
Escherichia coli
-
-
0.001
pimeloyl-CoA
Escherichia coli
-
-
0.004
pimeloyl-CoA
Mycobacterium tuberculosis
-
pH 7.7, 25C, recombinant enzyme
0.005
pimeloyl-CoA
Lysinibacillus sphaericus
-
-
0.1
pimeloyl-CoA
Arabidopsis thaliana
Q8GW43
pH 7.5, 30C, recombinant enzyme
0.5
pimeloyl-CoA
Lysinibacillus sphaericus
-
-
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.014
L-alanine
Symbiobacterium thermophilum
-
pH 6.0, 60C
103
0.11
L-alanine
Escherichia coli
-
5-aminolevulinate synthase-fusion protein (single chain chimeric dimer), pH 7.5, 30C
103
0.12
L-alanine
Escherichia coli
-
wild type protein, pH not specified in the publication, temperature not specified in the publication
103
0.984
L-alanine
Geobacillus kaustophilus
-
pH 6.0, 60C
103
7.33
L-alanine
Aquifex aeolicus
-
pH 6.0, 60C
103
1.5
pimeloyl-CoA
Symbiobacterium thermophilum
-
pH 6.0, 60C
2674
2.33
pimeloyl-CoA
Escherichia coli
-
wild type protein, pH not specified in the publication, temperature not specified in the publication
2674
2.4
pimeloyl-CoA
Escherichia coli
-
pH not specified in the publication, temperature not specified in the publication
2674
2.67
pimeloyl-CoA
Escherichia coli
-
5-aminolevulinate synthase-fusion protein (single chain chimeric dimer), pH 7.5, 30C
2674
4.9
pimeloyl-CoA
Geobacillus kaustophilus
-
pH 6.0, 60C
2674
213
pimeloyl-CoA
Aquifex aeolicus
-
pH 6.0, 60C
2674
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0017
(R)-8-amino-7-oxononanoic acid
-
competitive constant, pyridoxamine 5'-phosphate form of enzyme, coupled assay at 37C with 100 mM N-(2-hydroxyethyl)piperazine-N'-(2-propanesulfonic acid) buffer (pH 8.6), 10 mM ATP, 50 mM NaHCO3, 10 mM MgCl2, dithiobiotin syntetase, 0.1 mM pyridoxal 5'-phosphate, 2.5 mM S-adenosyl-L-methionine and various concentrations of (S)-8-amino-7-oxononanoic acid, 0.2-19.2 microM inhibitor
0.0033
(R)-8-amino-7-oxononanoic acid
-
uncompetitive constant, pyridoxal 5'-phosphate form of enzyme, coupled assay at 37C with 100 mM N-(2-hydroxyethyl)piperazine-N'-(2-propanesulfonic acid) buffer (pH 8.6), 10 mM ATP, 50 mM NaHCO3, 10 mM MgCl2, dithiobiotin syntetase, 0.1 mM pyridoxal 5'-phosphate, varicous concentrations of S-adenosyl-L-methionine and 9 microM (S)-8-amino-7-oxononanoic acid, 0.2-20 microM inhibitor
0.0059
(R)-8-amino-7-oxononanoic acid
-
competitive constant, pyridoxal 5'-phosphate form of enzyme, coupled assay at 37C with 100 mM N-(2-hydroxyethyl)piperazine-N'-(2-propanesulfonic acid) buffer (pH 8.6), 10 mM ATP, 50 mM NaHCO3, 10 mM MgCl2, dithiobiotin syntetase, 0.1 mM pyridoxal 5'-phosphate, varicous concentrations of S-adenosyl-L-methionine and 9 microM (S)-8-amino-7-oxononanoic acid, 0.2-57.3 microM inhibitor
0.0134
(R)-8-amino-7-oxononanoic acid
-
uncompetitive constant, pyridoxal 5'-phosphate form of enzyme, coupled assay at 37C with 100 mM N-(2-hydroxyethyl)piperazine-N'-(2-propanesulfonic acid) buffer (pH 8.6), 10 mM ATP, 50 mM NaHCO3, 10 mM MgCl2, dithiobiotin syntetase, 0.1 mM pyridoxal 5'-phosphate, varicous concentrations of S-adenosyl-L-methionine and 9 microM (S)-8-amino-7-oxononanoic acid, 0.2-57.3 microM inhibitor
0.0153
(R)-8-amino-7-oxononanoic acid
-
competitive constant, pyridoxal 5'-phosphate form of enzyme, coupled assay at 37C with 100 mM N-(2-hydroxyethyl)piperazine-N'-(2-propanesulfonic acid) buffer (pH 8.6), 10 mM ATP, 50 mM NaHCO3, 10 mM MgCl2, dithiobiotin syntetase, 0.1 mM pyridoxal 5'-phosphate, varicous concentrations of S-adenosyl-L-methionine and 9 microM (S)-8-amino-7-oxononanoic acid, 0.2-20 microM inhibitor
0.0162
(R)-8-amino-7-oxononanoic acid
-
uncompetitive constant, pyridoxamine 5'-phosphate form of enzyme, coupled assay at 37C with 100 mM N-(2-hydroxyethyl)piperazine-N'-(2-propanesulfonic acid) buffer (pH 8.6), 10 mM ATP, 50 mM NaHCO3, 10 mM MgCl2, dithiobiotin syntetase, 0.1 mM pyridoxal 5'-phosphate, 2.5 mM S-adenosyl-L-methionine and various concentrations of (S)-8-amino-7-oxononanoic acid, 0.2-19.2 microM inhibitor
0.08
2-amino-3-hydroxy-2-methylnonadioic acid
-
-
0.068
4-carboxybutyl(1-amino-1-carboxyethyl)phosphonate
-
-
0.007
8-amino-7-oxo-8-phosphonononanoic acid
-
-
0.0009
8-amino-7-oxooctanoic acid
-
achiral substrate analogue, competitive constant, pyridoxamine 5'-phosphate form of enzyme, coupled assay at 37C with 100 mM N-(2-hydroxyethyl)piperazine-N'-(2-propanesulfonic acid) buffer (pH 8.6), 10 mM ATP, 50 mM NaHCO3, 10 mM MgCl2, dithiobiotin syntetase, 0.1 mM pyridoxal 5'-phosphate, 2.5 mM S-adenosyl-L-methionine and varicous concentrations of (S)-8-amino-7-oxononanoic acid, 0-100 microM inhibitor
0.0042
8-amino-7-oxooctanoic acid
-
achiral substrate analogue, competitive constant, pyridoxal 5'-phosphate form of enzyme, coupled assay at 37C with 100 mM N-(2-hydroxyethyl)piperazine-N'-(2-propanesulfonic acid) buffer (pH 8.6), 10 mM ATP, 50 mM NaHCO3, 10 mM MgCl2, dithiobiotin syntetase, 0.1 mM pyridoxal 5'-phosphate, varicous concentrations of S-adenosyl-L-methionine and 9 microM (S)-8-amino-7-oxononanoic acid, 0-60 microM inhibitor
0.0125
8-amino-7-oxooctanoic acid
-
achiral substrate analogue, uncompetitive constant, pyridoxamine 5'-phosphate form of enzyme, coupled assay at 37C with 100 mM N-(2-hydroxyethyl)piperazine-N'-(2-propanesulfonic acid) buffer (pH 8.6), 10 mM ATP, 50 mM NaHCO3, 10 mM MgCl2, dithiobiotin syntetase, 0.1 mM pyridoxal 5'-phosphate, 2.5 mM S-adenosyl-L-methionine and varicous concentrations of (S)-8-amino-7-oxononanoic acid, 0-100 microM inhibitor
0.0152
8-amino-7-oxooctanoic acid
-
achiral substrate analogue, uncompetitive constant, pyridoxal 5'-phosphate form of enzyme, coupled assay at 37C with 100 mM N-(2-hydroxyethyl)piperazine-N'-(2-propanesulfonic acid) buffer (pH 8.6), 10 mM ATP, 50 mM NaHCO3, 10 mM MgCl2, dithiobiotin syntetase, 0.1 mM pyridoxal 5'-phosphate, varicous concentrations of S-adenosyl-L-methionine and 9 microM (S)-8-amino-7-oxononanoic acid, 0-60 microM inhibitor
0.59
D-alanine
-
-
1.24
D-alanine
-
-
3.75
D-histidine
-
-
0.115
D-KAPA
-
pH 7.7, 25C, recombinant enzyme
0.99
L-cysteine
-
-
5.6
L-histidine
-
-
additional information
additional information
-
dimethyl-8-amino-7-oxooctanoic acid, an achiral substrate analogue, does not inhibit the enzyme
-
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.011
2,3-dichloronaphthalene-1,4-dione
Arabidopsis thaliana
-
pH 7.5, 30C
0.042
2-(furan-2-yl)-1H-benzimidazole
Arabidopsis thaliana
-
pH 7.5, 30C
0.056
2-[(1,1,2,2-tetrachloroethyl)sulfanyl]-3a,4,7,7a-tetrahydro-1H-isoindole-1,3(2H)-dione
Arabidopsis thaliana
-
pH 7.5, 30C
0.054
2-[(trichloromethyl)sulfanyl]-3a,4,7,7a-tetrahydro-1H-isoindole-1,3(2H)-dione
Arabidopsis thaliana
-
pH 7.5, 30C
0.0013
4-(1H-inden-3-yl)naphthalene-1,2-dione
Arabidopsis thaliana
-
pH 7.5, 30C
0.011
5,10-dioxo-5,10-dihydronaphtho[2,3-b][1,4]dithiine-2,3-dicarbonitrile
Arabidopsis thaliana
-
pH 7.5, 30C
0.0044
5,8-dihydronaphthalene-1,4-dione
Arabidopsis thaliana
-
pH 7.5, 30C
0.0044
5,8-dihydroxynaphthalene-1,4-dione
Arabidopsis thaliana
-
pH 7.5, 30C
0.0021
5-hydroxy-2-methylnaphthalene-1,4-dione
Arabidopsis thaliana
-
pH 7.5, 30C
0.0096
5-hydroxynaphthalene-1,4-dione
Arabidopsis thaliana
-
pH 7.5, 30C
0.0044
methyl 3-(5,6-dioxo-5,6-dihydronaphthalen-2-yl)propanoate
Arabidopsis thaliana
-
pH 7.5, 30C
0.0011
methyl 3-[8-(1H-inden-3-yl)-5,6-dioxo-5,6-dihydronaphthalen-2-yl]propanoate
Arabidopsis thaliana
-
pH 7.5, 30C
0.00063
methyl 3-[8-[(4-fluorophenyl)amino]-5,6-dioxo-5,6-dihydronaphthalen-2-yl]propanoate
Arabidopsis thaliana
-
pH 7.5, 30C
0.00059
methyl 3-[8-[(4-methylphenyl)amino]-5,6-dioxo-5,6-dihydronaphthalen-2-yl]propanoate
Arabidopsis thaliana
-
pH 7.5, 30C
0.041
N-[dichloro(fluoro)-l4-sulfanyl]-N',N'-dimethyl-N-phenylsulfuric diamide
Arabidopsis thaliana
-
pH 7.5, 30C
0.047
N-[dichloro(fluoromethyl)-lambda4-sulfanyl]-N',N'-dimethyl-N-(4-methylphenyl)sulfuric diamide
Arabidopsis thaliana
-
pH 7.5, 30C
0.0033
naphthalene-1,2-dione
Arabidopsis thaliana
-
pH 7.5, 30C
0.01985
triphenyltin acetate
Arabidopsis thaliana
-
pH 7.5, 37C
-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0.00225
-
partially purified enzyme
0.032
-
glycine, pimeloyl-CoA, pH 6.0, 60C
0.071
-
L-alanine, pimeloyl-CoA, pH 6.0, 60C
0.078
-
L-alanine, pimeloyl-CoA, pH 6.0, 60C
0.09 - 0.1
purified recombinant enzyme
0.272
-
L-alanine, acetyl-CoA, pH 6.0, 60C
0.897
-
glycine, acetyl-CoA, pH 6.0, 60C
2.46
-
L-alanine, pimeloyl-CoA, pH 6.0, 60C
additional information
-
crude cell-extracts from various organism
additional information
-
activity in biotin mutants
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7
-
assay at
7.5
-
assay at
additional information
-
pI: 5.2
additional information
-
pI: 7.0
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6.3 - 7.6
-
-
6.5 - 7.5
-
about half-maximal activity at pH 6.5 and pH 7.5
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
45 - 65
-
about half-maximal activity at 45C and 65C
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
-
expressed in most tissue
Manually annotated by BRENDA team
-
expressed in most tissue
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
PDB
SCOP
CATH
ORGANISM
UNIPROT
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Francisella tularensis subsp. tularensis (strain SCHU S4 / Schu 4)
Mycobacterium smegmatis (strain ATCC 700084 / mc(2)155)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
41000
-
-
487056
41600
-
calculated from nucleotide sequence
487049
41740
-
electrospray mass spectrometry, holoenzyme
487058
46000
-
gel filtration
487048
50000
recombinant His-tagged enzyme, gel filtration
676580
additional information
-
amino acid composition
487048
additional information
-
amino acid sequence
487049, 487057
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
?
-
x * 42000, recombinant His-tagged enzyme, SDS-PAGE, x * 42249, recombinant His-tagged enzyme, mass spectrometry, x * 42194, amino acid sequence calculation
?
-
x * 45000, SDS-PAGE
?
-
x * 45000, SDS-PAGE
?
-
x * 46000, SDS-PAGE
?
-
x * 45000, SDS-PAGE
?
-
x * 51300, calculated from 98200, SDS-PAGE of maltose binding protein fusion protein
?
Geobacillus kaustophilus JCM12893
-
x * 44000, SDS-PAGE
-
?
Ruminiclostridium thermocellum ATCC27405
-
x * 45000, SDS-PAGE
-
?
Symbiobacterium thermophilum IAM14863
-
x * 46000, SDS-PAGE
-
dimer
-
2 * ?
dimer
-
2 * ?, modeling with Escherichia coli enzyme as template
dimer
Escherichia coli C268
-
2 * ?
-
homodimer
-
2 x 40000, SDS-PAGE
monomer
-
1 * 41000, SDS-PAGE
monomer
-
1 * 41690, native enzyme with bound cofactor, mass spectrometry
monomer
1 * 52171, amino acid sequence calculation
additional information
-
homodimer with each monomer consisting of 3 domains
additional information
-
dimer, active site is formed at the interface between the monomers
additional information
-
comparison of the AONS active site in the apo-enzyme, the holo-enzyme, the difluoro-adduct, and the product aldimine, overview
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
enzyme in complex with inhibitor trifluoroalanine, soaking of holo-enzyme crystals in a solution containing 10 mM L-trifluoroalanine and 10 mM pyridoxal-5'-phosphate in crystallization buffer containing 1.6 M ammonium sulfate and 200 mM 1,3-bis[tris(hydroxymethyl)methylamino]propane at pH 8.5, and rapidly frozen in liquid nitrogen, X-ray diffraction structure determination and analysis at 1.99 A resolution
-
Mg2+ added for structure analysis of the holoenzyme; pH 8.5-8.9, ammonium sulfate precipitation, apoenzyme, X-ray diffraction structure analysis with and without bound pyridoxyl-5'-phosphate, model, active site residues
-
pH 8.5-8.9, ammonium sulfate precipitation, apoenzyme, X-ray diffraction structure analysis with and without bound pyridoxyl-5'-phosphate, model, active site residues
-
pyridoxal-5'-phosphate-bound form, pH 7.5, precipitation with polyethylene glycol, 0.2 M (NH4)2SO4 , x-ray diffraction structure analysis
-
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
40
-
stable for one h
719127
55
-
stable for one h
719127
60
-
and below, stable
487052
65
-
stable for one h
719127
70
-
t1/2: 10 min
487052
70
-
stable for one h
719127
75
-
stable for one h
719127
80
-
and above, inactivation
487052
93
-
stable for one h
719127
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
EDTA stabilizes during purification
-
freeze-thawing inactivates
-
proteinase inhibitors, e.g. PMSF, pepstatin A, stabilize during purification
-
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20C, 0.01 M phosphate buffer, pH 7.0, 5 mM 2-mercaptoethanol, 5 months
-
0C, several months
-
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
Glutathione Sepharose chromatography, GST-tag cleavage, Glutathione Sepharose chromatography, gel filtration
-
maltose binding protein affinity chromatography
-
native enzyme partially by subcellular fractionation, recombinant His-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography and gel filtration
from Escherichia coli DH5alpha, ammonium sulfate fractionation, gel filtration, hydrophobic interaction chromatography, ion exchange chromatography
-
Glutathione Sepharose chromatography, GST-tag cleavage, Glutathione Sepharose chromatography, ion exchange chromatography
-
recombinant from E. coli
-
recombinant from overexpressing E. coli strain HMS174 (DE3)
-
Glutathione Sepharose chromatography, GST-tag cleavage, Glutathione Sepharose chromatography, ion exchange chromatography
-
partial; recombinant from E. coli overproducing strain
-
recombinant from E. coli overproducing strain
-
recombinant His-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affiinity chromatography and gel filtration to homogeneity
-
Glutathione Sepharose chromatography, GST-tag cleavage, Glutathione Sepharose chromatography
-
Glutathione Sepharose chromatography, GST-tag cleavage, Glutathione Sepharose chromatography, heat treatment with centrifugation
-
immobilized metal ion affinity chromatography (Ni2+), His-tag cleavage, immobilized metal ion affinity chromatography (Ni2+), gel filtration
-
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
GST-fusion protein expressed in Escherichia coli JM109
-
gene bioF, DNA and amino acid sequence determination and analysis, overexpression of His-tagged enzyme in Escherichia coli strain BL21(DE3)
maltose binding protein fusion protein expressed in Escherichia coli BL21-Gold(DE3)
-
bioF gene overexpression in Escherichia coli
-
bioF gene, expression in strain HMS174 (DE3)
-
GST-fusion protein expressed in Escherichia coli JM109
-
His-tagged protein and murine 5-aminolevulinate synthase-fusion protein (single chain chimeric dimer) expressed in Escherichia coli HU227, R872 and DH5alpha
-
histidine-tagged enzyme is expressed in Escherichia coli C268
-
GST-fusion protein expressed in Escherichia coli JM109
-
expressed in overproducing Escherichia coli strain C268/pTG3401
-
improved overexpression in Escherichia coli bioF- strain R874
-
gene Rv1569, overexpression of His-tagged enzyme in Escherichia coli strain BL21(DE3)
-
histidine-tagged enzyme is expressed in Escherichia coli C268
-
GST-fusion protein expressed in Escherichia coli JM109
-
His-tagged protein expressed in Escherichia coli Rosetta-gami (DE3)
-
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
functional complementation of an Escherichia coli mutant deficient in KAPA synthase reaction
K236A
-
active site lysine involved in the Schiff base linkage with the PLP cofactor
additional information
-
natural mutants with altered enzyme activity
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
medicine
-
enzyme is a potential target for antimycobacterial drugs
medicine
Escherichia coli C268
-
enzyme is a potential target for antimycobacterial drugs
-
agriculture
-
possible target for design of inhibitors as herbicides and antibacterial agents
medicine
-
enzyme is a potential target for antimycobacterial drugs