Any feedback?
Information on EC 2.3.1.29 - glycine C-acetyltransferase
for references in articles please use BRENDA:EC2.3.1.29Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EC Tree
2.3.1.29 glycine C-acetyltransferaseIUBMB Comments
This is a pyridoxal-phosphate-dependent enzyme that acts in concert with EC 1.1.1.103, L-threonine 3-dehydrogenase, in the degradation of threonine to form glycine . This threonine degradation pathway is common to prokaryotic and eukaryotic cells and the two enzymes involved form a complex .
Specify your search results
Word Map
- 2.3.1.29
- l-threonine
- pyridoxal
- 5'-phosphate
- 5-aminolevulinate
-
1.1.1.103
- 8-amino-7-oxononanoate
-
5'-phosphate-dependent
-
7-keto-8-aminopelargonic
-
biofs
- synthesis
The expected taxonomic range for this enzyme is: Bacteria, Archaea, Eukaryota
Synonyms
aminoacetone synthetase, 2-amino-3-ketobutyrate coa ligase, 2-amino-3-ketobutyrate coenzyme a ligase, aminoacetone synthase, 2-amino-3-ketobutyrate-coa ligase, glycine c-acetyltransferase, 2-amino-3-oxobutyrate coa ligase, glycine acetyltransferase, 
more
topPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
2-amino-3-ketobutyrate CoA ligase
2-amino-3-ketobutyrate coenzyme A ligase
-
-
-
-
2-amino-3-ketobutyrate-CoA ligase
-
-
-
-
acetyltransferase, glycine
-
-
-
-
alpha-amino-beta-oxobutyrate CoA-ligase
-
-
-
-
aminoacetone synthase
-
-
-
-
aminoacetone synthetase
-
-
-
-
glycine acetyltransferase
-
-
-
-
KBL
2-amino-3-ketobutyrate CoA ligase
-
-
-
-
KBL
-
enzyme is found to catalyze also the 7-keto-8-aminopelargnic acid (KAPA) synthase reaction
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
acetyl-CoA + glycine = CoA + L-2-amino-3-oxobutanoate
reaction mechanism
acetyl-CoA + glycine = CoA + L-2-amino-3-oxobutanoate
physical interaction between threonine dehydrogenase and aminoacetone synthetase demonstrated, the two enzymes form a complex
-
acetyl-CoA + glycine = CoA + L-2-amino-3-oxobutanoate
the condensation process involves the loss of the pro-R hydrogen atom of glycine and occurs with the inversion of stereochemistry
-
acetyl-CoA + glycine = CoA + L-2-amino-3-oxobutanoate
-
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Acyl group transfer
-
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
PATHWAY SOURCE
PATHWAYS
BRENDA
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SYSTEMATIC NAME
IUBMB Comments
acetyl-CoA:glycine C-acetyltransferase
This is a pyridoxal-phosphate-dependent enzyme that acts in concert with EC 1.1.1.103, L-threonine 3-dehydrogenase, in the degradation of threonine to form glycine [3]. This threonine degradation pathway is common to prokaryotic and eukaryotic cells and the two enzymes involved form a complex [4].
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
CAS REGISTRY NUMBER
COMMENTARY
37257-11-7
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
acetyl-CoA + aminomalonate
CoA + CO2 + 2-amino-3-oxobutanoate
-
-
same product as in reaction with glycine, aminomalonate is decarboxylated to glycine by the enzyme, in the absence of acetyl-CoA: glycine is the product
?
n-butyryl-CoA + glycine
CoA + 2-amino-3-oxohexanoate
-
reaction at 16% the rate of acetyl-CoA
-
-
?
n-propionyl-CoA + glycine
CoA + 2-amino-3-oxopentanoate
-
reaction at 127% the rate of acetyl-CoA
-
-
?
additional information
?
-
-
the enzyme catalyzes the exchange of pro-R hydrogen of glycine with protons in the medium
-
-
?
acetyl-CoA + glycine
CoA + 2-amino-3-oxobutanoate
-
-
spontaneous decarboxylation to aminoacetone
?
acetyl-CoA + glycine
CoA + 2-amino-3-oxobutanoate
-
involved in L-threonine catabolism, inducible
-
?
acetyl-CoA + glycine
CoA + 2-amino-3-oxobutanoate
-
-
spontaneous decarboxylation to aminoacetone
r
acetyl-CoA + glycine
CoA + 2-amino-3-oxobutanoate
-
-
spontaneous decarboxylation to aminoacetone
r
acetyl-CoA + glycine
CoA + 2-amino-3-oxobutanoate
-
specific for glycine
spontaneous decarboxylation to aminoacetone
r
acetyl-CoA + glycine
CoA + 2-amino-3-oxobutanoate
-
succinyl-CoA
spontaneous decarboxylation to aminoacetone
r
acetyl-CoA + glycine
CoA + 2-amino-3-oxobutanoate
-
not: acetyl phosphate
spontaneous decarboxylation to aminoacetone
r
acetyl-CoA + glycine
CoA + 2-amino-3-oxobutanoate
-
no substrate: L-alanine
spontaneous decarboxylation to aminoacetone
r
acetyl-CoA + glycine
CoA + 2-amino-3-oxobutanoate
-
no substrate: glycine methylester
spontaneous decarboxylation to aminoacetone
r
acetyl-CoA + glycine
CoA + 2-amino-3-oxobutanoate
-
acetyl-CoA cannot be replaced by acetyl phosphate
spontaneous decarboxylation to aminoacetone
r
acetyl-CoA + glycine
CoA + 2-amino-3-oxobutanoate
-
involved in L-threonine catabolism, inducible
-
?
acetyl-CoA + glycine
CoA + 2-amino-3-oxobutanoate
-
involved in L-threonine catabolism, inducible
-
?
acetyl-CoA + glycine
CoA + 2-amino-3-oxobutanoate
-
involved in L-threonine catabolism, inducible
-
-
?
acetyl-CoA + glycine
CoA + 2-amino-3-oxobutanoate
-
enzyme catalyzes the second reaction step on the main metabolic degradation pathway for threonine
-
-
?
acetyl-CoA + glycine
CoA + 2-amino-3-oxobutanoate
-
spontaneous decarboxylation to aminoacetone
?
acetyl-CoA + glycine
CoA + 2-amino-3-oxobutanoate
-
not: valeryl-CoA, glutaryl-CoA
-
-
r
acetyl-CoA + glycine
CoA + 2-amino-3-oxobutanoate
-
specific for glycine
-
-
?
acetyl-CoA + glycine
CoA + 2-amino-3-oxobutanoate
-
specific for glycine
-
-
r
acetyl-CoA + glycine
CoA + 2-amino-3-oxobutanoate
-
no substrate: L-alanine
-
-
r
acetyl-CoA + glycine
CoA + 2-amino-3-oxobutanoate
-
no substrates: glycinamide, 2-aminoethanol, aminomethylphosphonic acid, aminomalonate
-
-
r
acetyl-CoA + glycine
CoA + 2-amino-3-oxobutanoate
-
no substrate: glycine methylester
-
-
r
acetyl-CoA + glycine
CoA + 2-amino-3-oxobutanoate
-
no substrates: L-serine, L-threonine, L-valine, L-leucine
-
-
r
acetyl-CoA + glycine
CoA + 2-amino-3-oxobutanoate
-
involved in L-threonine catabolism, inducible
-
-
?
acetyl-CoA + glycine
CoA + 2-amino-3-oxobutanoate
enzyme catalyzes the second reaction step on the main metabolic degradation pathway for threonine
-
-
?
acetyl-CoA + glycine
CoA + 2-amino-3-oxobutanoate
-
the condensation process involves the loss of the pro-R hydrogen atom of glycine and occurs with the inversion of stereochemistry
-
-
?
acetyl-CoA + glycine
CoA + 2-amino-3-oxobutanoate
-
-
spontaneous decarboxylation to aminoacetone
r
acetyl-CoA + glycine
CoA + 2-amino-3-oxobutanoate
-
enzyme catalyzes the second reaction step on the main metabolic degradation pathway for threonine
-
-
?
acetyl-CoA + glycine
CoA + 2-amino-3-oxobutanoate
-
-
spontaneous decarboxylation to aminoacetone
r
acetyl-CoA + glycine
CoA + 2-amino-3-oxobutanoate
-
enzyme catalyzes the second reaction step on the main metabolic degradation pathway for threonine
-
-
?
acetyl-CoA + glycine
CoA + 2-amino-3-oxobutanoate
-
involved in L-threonine catabolism, inducible
-
-
?
acetyl-CoA + glycine
CoA + L-2-amino-3-oxobutanoate
-
condensation reaction
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
acetyl-CoA + glycine
CoA + L-2-amino-3-oxobutanoate
-
condensation reaction
-
-
?
acetyl-CoA + glycine
CoA + 2-amino-3-oxobutanoate
-
involved in L-threonine catabolism, inducible
-
?
acetyl-CoA + glycine
CoA + 2-amino-3-oxobutanoate
-
involved in L-threonine catabolism, inducible
-
?
acetyl-CoA + glycine
CoA + 2-amino-3-oxobutanoate
-
involved in L-threonine catabolism, inducible
-
?
acetyl-CoA + glycine
CoA + 2-amino-3-oxobutanoate
-
involved in L-threonine catabolism, inducible
-
-
?
acetyl-CoA + glycine
CoA + 2-amino-3-oxobutanoate
-
enzyme catalyzes the second reaction step on the main metabolic degradation pathway for threonine
-
-
?
acetyl-CoA + glycine
CoA + 2-amino-3-oxobutanoate
-
involved in L-threonine catabolism, inducible
-
-
?
acetyl-CoA + glycine
CoA + 2-amino-3-oxobutanoate
enzyme catalyzes the second reaction step on the main metabolic degradation pathway for threonine
-
-
?
acetyl-CoA + glycine
CoA + 2-amino-3-oxobutanoate
-
enzyme catalyzes the second reaction step on the main metabolic degradation pathway for threonine
-
-
?
acetyl-CoA + glycine
CoA + 2-amino-3-oxobutanoate
-
enzyme catalyzes the second reaction step on the main metabolic degradation pathway for threonine
-
-
?
acetyl-CoA + glycine
CoA + 2-amino-3-oxobutanoate
-
involved in L-threonine catabolism, inducible
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
pyridoxal 5'-phosphate
-
pyridoxal 5'-phosphate is covalently bound to an active site lysine, formation of a Schiff base
pyridoxal 5'-phosphate
-
requirement, stoichiometry: 1 mol per mol subunit
pyridoxal 5'-phosphate
-
location of pyridoxyllysine peptide in primary structure of enzyme
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Phenylglyoxal
-
inactivation, 50% protection by pyridoxal 5'-phosphate or CoA (glycine or threonine to some extent), kinetics
additional information
-
no inhibition by DTNB; not: PCMB, glycine methylester, glycinamide
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
additional information
-
kinetics of the exchange of pro-R hydrogen of glycine with protons in the medium by the enzyme
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7.5
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
by using inducible translocation trap (ITT), a reporter gene-based screening technique, nuclear translocation of 2-amino-3-ketobutyrate coenzyme A ligase (KBL) is detected in response to cold and osmotic stresses
brenda
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
-
2-amino-3-ketobutyrate CoA ligase of Escherichia coli is a member of the alpha-oxoamine synthase family
Show AA Sequence and Transmembrane Helices (13831 entries)
Longer loading times are possible. Please use the AA Sequence and Transmembrane Helices Search for a specific query.
Longer loading times are possible. Please use the AA Sequence and Transmembrane Helices Search for a specific query.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
PDB
SCOP
CATH
UNIPROT
ORGANISM
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
41690
-
2 * 41690, gel filtration, denaturating conditions, 2 * 41930, SDS-PAGE, 2 * 42093, calculated from amino acid composition
41930
-
2 * 41690, gel filtration, denaturating conditions, 2 * 41930, SDS-PAGE, 2 * 42093, calculated from amino acid composition
42093
-
2 * 41690, gel filtration, denaturating conditions, 2 * 41930, SDS-PAGE, 2 * 42093, calculated from amino acid composition
43000
56000
84190
85000
additional information
43000
-
x * 43117.15, recombinant enzyme, mass spectrometry, x * 43000, recombinant enzyme, SDS-PAGE
additional information
-
when loaded together threonine dehydrogease and aminoacetone synthetase co-eludes at a molecular weight of 150000 Da
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
?
-
x * 43117.15, recombinant enzyme, mass spectrometry, x * 43000, recombinant enzyme, SDS-PAGE
dimer
monomer
additional information
-
the threonine dehydrogenase and the aminoacetone synthetase form a complex with an apparent stoichiometry of two dimers of aminoacetone synthetase to one threonine dehydrogenase tetramer
dimer
-
2 * 41690, gel filtration, denaturating conditions, 2 * 41930, SDS-PAGE, 2 * 42093, calculated from amino acid composition
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
side-chain modification
-
the phenylglyoxal-inactivated enzyme is associated with the loss of 1.5 arginine residue per ligase subunit
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
external aldimine in the crystal structure, interaction between aldimine and the side chains in the substrate binding site explain the specificity to the substrate
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
-
enzyme shows high thermostability at 70°C for 1 h and a half-life of 1 h at 80°C
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
glycerol, 10% v/v, stabilizes
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant enzyme by ammonium sulfate fractionation, anion exchange and hydrophobic interaction chromatography, followed by gel filtration
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
bovine partial
expressed in Escherichia coli
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
synthesis
synthesis
-
enzyme is applied in synthesis of 2,5-dimethylpyrazine. Bacillus subtilis can synthesize 2,5-dimethylpyrazine by using L-threonine as the substrate via aminoacetone. The reaction from L-threonine to L-2-amino-acetoacetate is catalyzed by L-threonine-3-dehydrogenase. L-2-Amino-acetoacetate can spontaneously decarboxylate to form aminoacetone. The reaction from aminoacetone to 2,5-dimethylpyrazine is a pH-dependent nonenzymatic reaction. Inactivation of 2-amino-3-ketobutyrate CoA ligase improves 2,5-dimethylpyrazine production
synthesis
-
enzyme is applied in synthesis of 2,5-dimethylpyrazine. Bacillus subtilis can synthesize 2,5-dimethylpyrazine by using L-threonine as the substrate via aminoacetone. The reaction from L-threonine to L-2-amino-acetoacetate is catalyzed by L-threonine-3-dehydrogenase. L-2-Amino-acetoacetate can spontaneously decarboxylate to form aminoacetone. The reaction from aminoacetone to 2,5-dimethylpyrazine is a pH-dependent nonenzymatic reaction. Inactivation of 2-amino-3-ketobutyrate CoA ligase improves 2,5-dimethylpyrazine production
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Tressel, T.; Thompson, R.; Zieske, L.R.; Menendez, M.I.T.S.; Davis, L.
Interaction between L-threonine dehydrogenase and aminoacetone synthetase and mechanism of aminoacetone production
J. Biol. Chem.
261
16428-16437
1986
Sus scrofa
brenda
McGilvray, D.; Morris, J.G.
Utilization of L-threonine by a species of Arthrobacter. A novel catabolic role for aminoacetone synthase
Biochem. J.
112
657-671
1969
Arthrobacter sp.
brenda
Mukherjee, J.J.; Dekker, E.E.
Purification, properties, and N-terminal amino acid sequence of homogeneous Escherichia coli 2-amino-3-ketobutyrate CoA ligase, a pyridoxal phosphate-dependent enzyme
J. Biol. Chem.
262
14441-14447
1987
Escherichia coli
brenda
Mukherjee, J.J.; Dekker, E.E.
Inactivation of Escherichia coli 2-amino-3-ketobutyrate CoA ligase by phenylglyoxal and identification of an active-site arginine peptide
Arch. Biochem. Biophys.
299
147-153
1992
Escherichia coli
brenda
Mukherjee, J.J.; Dekker, E.E.
2-Amino-3-ketobutyrate CoA ligase of Escherichia coli: stoichiometry of pyridoxal phosphate binding and location of the pyridoxyllysine peptide in the primary structure of the enzyme
Biochim. Biophys. Acta
1037
24-29
1990
Escherichia coli
brenda
Aronson, B.D.; Ravnikar, P.D.; Somerville, R.L.
Nucleotide sequence of the 2-amino-3-ketobutyrate coenzyme A ligase (kbl) gene of E. coli
Nucleic Acids Res.
16
3586
1988
Escherichia coli (P0AB77)
brenda
Fubara, B.; Eckenrode, F.; Tressel, T.; Davis, L.
Purification and properties of aminoacetone synthetase from beef liver mitochondria
J. Biol. Chem.
261
12189-12196
1986
Bos taurus
brenda
Tong, H.; Davis, L.
2-Amino-3-ketobutyrate-CoA ligase from beef liver mitochondria. Purification and partial sequence
J. Biol. Chem.
269
4057-4064
1994
Bos taurus
brenda
Tong, H.; Davis, L.
2-Amino-3-ketobutyrate-CoA ligase from beef liver mitochondria: An NMR spectroscopic study of low-barrier hydrogen bonds of a pyridoxal 5'-phosphate-dependent enzyme
Biochemistry
34
3362-3367
1995
Bos taurus
brenda
Edgar, A.J.; Polak, J.M.
Molecular cloning of the human and murine 2-amino-3-ketobutyrate coenzyme A ligase cDNAs
Eur. J. Biochem.
267
1805-1812
2000
Bos taurus, Homo sapiens, Mus musculus, Escherichia coli (P0AB77), Escherichia coli
brenda
Bashir, Q.; Rashid, N.; Akhtar, M.
Mechanism and substrate stereochemistry of 2-amino-3-oxobutyrate CoA ligase: implications for 5-aminolevulinate synthase and related enzymes
Chem. Commun. (Camb. )
2006
5065-5067
2006
Escherichia coli
brenda
Kubota, T.; Shimono, J.; Kanameda, C.; Izumi, Y.
The first thermophilic alpha-oxoamine synthase family enzyme that has activities of 2-amino-3-ketobutyrate CoA ligase and 7-keto-8-aminopelargonic acid synthase: cloning and overexpression of the gene from an extreme thermophile, Thermus thermophilus, and
Biosci. Biotechnol. Biochem.
71
3033-3040
2007
Thermus thermophilus
brenda
Hoshino, A.; Fujii, H.
Nuclear translocation of 2-amino-3-ketobutyrate coenzyme A ligase by cold and osmotic stress
Cell Stress Chaperones
12
186-191
2007
Mus musculus
brenda
Jamil, F.
Kinetics of the exchange reaction catalyzed by 2-amino-3-ketobutyrate CoA ligase
Front. Biol.
10
503-507
2015
Escherichia coli
-
brenda
Zhang, L.; Cao, Y.; Tong, J.; Xu, Y.
An alkylpyrazine synthesis mechanism involving L-threonine-3-dehydrogenase describes the production of 2,5-dimethylpyrazine and 2,3,5-trimethylpyrazine by Bacillus subtilis
Appl. Environ. Microbiol.
85
e01807
2019
Bacillus subtilis, Bacillus subtilis 168
brenda
Select items on the left to see more content.
EXTERNAL LINKS (specific for EC-Number 2.3.1.29)
html completed
Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.
Release 2023.1 (January 2023)
About BRENDA
Social media
Help
Survey
Download
Contribution
Legal
Curated at
Member of
