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Information on EC 6.3.3.3 - dethiobiotin synthase
for references in articles please use BRENDA:EC6.3.3.3
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EC Tree 6 Ligases
6.3 Forming carbon-nitrogen bonds
6.3.3 Cyclo-ligases
6.3.3.3 dethiobiotin synthase
IUBMB Comments
CTP has half the activity of ATP.
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
- 6.3.3.3
-
7,8-diaminopelargonic
- aminotransferase
-
dapas
-
penultimate
-
ureido
- carbamate
-
diaminopelargonic
showSynonyms
dethiobiotin synthetase, dethiobiotin synthase, more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
BioD
Desthiobiotin synthetase
-
-
-
-
Dethiobiotin synthase
-
-
-
-
Dethiobiotin synthetase
DTB synthetase
-
-
-
-
DTBS
Synthetase, dethiobiotin
-
-
-
-
Dethiobiotin synthetase
-
-
-
-
DTBS
-
-
-
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
ATP + 7,8-diaminononanoate + CO2 = ADP + phosphate + dethiobiotin
the final intermediate is the phosphoric acid anhydride of the carbamate
-
ATP + 7,8-diaminononanoate + CO2 = ADP + phosphate + dethiobiotin
mechanistic model in which binding of Mg2+ and the triphosphate element of ATP to the enzyme creates the appropriate geometry for substrate 7,8-diaminononanoate-binding and carbamate formation
-
ATP + 7,8-diaminononanoate + CO2 = ADP + phosphate + dethiobiotin
8-aminocarbamate of (7R,8S)-7,8 diaminononanoate is an enzyme-bound intermediate
-
ATP + 7,8-diaminononanoate + CO2 = ADP + phosphate + dethiobiotin
the carbonylation of 7,8-diaminononanoic acid proceeds regiospecifically via the N7-carbamate
-
ATP + 7,8-diaminononanoate + CO2 = ADP + phosphate + dethiobiotin
enzyme reaction involves three steps: carbamylation of theN7 position of 7,8-diaminononanoate, formation of a carbamate-phosphoric anhydride intermediate, and, closure of the ureido ring to form dethiobiotin and release of the inorganic phosphate
-
ATP + 7,8-diaminononanoate + CO2 = ADP + phosphate + dethiobiotin
-
-
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
carboxylation
-
-
-
-
heteroatomic ring closure
-
-
-
-
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PATHWAY SOURCE
PATHWAYS
BRENDA
KEGG
MetaCyc
biotin biosynthesis from 8-amino-7-oxononanoate I, biotin biosynthesis from 8-amino-7-oxononanoate II
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SYSTEMATIC NAME
IUBMB Comments
7,8-diaminononanoate:carbon-dioxide cyclo-ligase (ADP-forming)
CTP has half the activity of ATP.
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CAS REGISTRY NUMBER
COMMENTARY
37259-75-9
-
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
ADP + 7,8-diaminononanoate + CO2
AMP + phosphate + dethiobiotin
-
Substrates: 5% of the activity relative to ATP
Products: -
Products: -
?
ATP + (7R,8S)-7,8-diaminopelargonic acid + NaHCO3
ADP + phosphate + dethiobiotin + Na+ + OH-
ATP + 7,8-diaminononanoate + CO2
?
-
Substrates: penultimate enzyme of biotin biosynthesis
Products: -
Products: -
?
CTP + (7R,8S)-7,8-diaminopelargonic acid + NaHCO3
CDP + phosphate + dethiobiotin + Na+ + OH-
GTP + (7R,8S)-7,8-diaminopelargonic acid + NaHCO3
GDP + phosphate + dethiobiotin + Na+ + OH-
GTP + 7,8-diaminononanoate + CO2
GDP + phosphate + dethiobiotin
Pseudomonas graveolens
-
Substrates: -
Products: -
Products: -
?
ITP + (7R,8S)-7,8-diaminopelargonic acid + NaHCO3
IDP + phosphate + dethiobiotin + Na+ + OH-
TTP + (7R,8S)-7,8-diaminopelargonic acid + NaHCO3
TDP + phosphate + dethiobiotin + Na+ + OH-
UTP + (7R,8S)-7,8-diaminopelargonic acid + NaHCO3
UDP + phosphate + dethiobiotin + Na+ + OH-
ATP + (7R,8S)-7,8-diaminopelargonic acid + NaHCO3
ADP + phosphate + dethiobiotin + Na+ + OH-
Substrates: -
Products: -
Products: -
?
ATP + (7R,8S)-7,8-diaminopelargonic acid + NaHCO3
ADP + phosphate + dethiobiotin + Na+ + OH-
Substrates: -
Products: -
Products: -
?
ATP + (7R,8S)-7,8-diaminopelargonic acid + NaHCO3
ADP + phosphate + dethiobiotin + Na+ + OH-
Substrates: -
Products: -
Products: -
?
ATP + 7,8-diaminononanoate + CO2
ADP + phosphate + dethiobiotin
-
Substrates: -
Products: -
Products: -
?
ATP + 7,8-diaminononanoate + CO2
ADP + phosphate + dethiobiotin
Substrates: third step in the biosynthesis of biotin, overview
Products: -
Products: -
?
ATP + 7,8-diaminononanoate + CO2
ADP + phosphate + dethiobiotin
Substrates: -
Products: -
Products: -
?
ATP + 7,8-diaminononanoate + CO2
ADP + phosphate + dethiobiotin
Bacillus roseus
-
Substrates: -
Products: -
Products: -
?
ATP + 7,8-diaminononanoate + CO2
ADP + phosphate + dethiobiotin
-
Substrates: -
Products: -
Products: -
?
ATP + 7,8-diaminononanoate + CO2
ADP + phosphate + dethiobiotin
-
Substrates: -
Products: -
Products: -
?
ATP + 7,8-diaminononanoate + CO2
ADP + phosphate + dethiobiotin
-
Substrates: -
Products: -
Products: -
?
ATP + 7,8-diaminononanoate + CO2
ADP + phosphate + dethiobiotin
-
1333, 1334, 1337, 1338, 1339, 1340, 1343, 1346, 1347, 1348, 1349, 1350, 1353, 653958, 649107, 653820
Substrates: -
Products: -
Products: -
?
ATP + 7,8-diaminononanoate + CO2
ADP + phosphate + dethiobiotin
-
Substrates: penultimate step in biotin biosynthesis
Products: -
Products: -
?
ATP + 7,8-diaminononanoate + CO2
ADP + phosphate + dethiobiotin
-
Substrates: CO2 in form of HCO3-
Products: -
Products: -
?
ATP + 7,8-diaminononanoate + CO2
ADP + phosphate + dethiobiotin
-
Substrates: -
Products: -
Products: -
?
ATP + 7,8-diaminononanoate + CO2
ADP + phosphate + dethiobiotin
-
Substrates: -
Products: -
Products: -
?
ATP + 7,8-diaminononanoate + CO2
ADP + phosphate + dethiobiotin
-
Substrates: -
Products: -
Products: -
?
ATP + 7,8-diaminononanoate + CO2
ADP + phosphate + dethiobiotin
-
Substrates: -
Products: -
Products: -
?
ATP + 7,8-diaminononanoate + CO2
ADP + phosphate + dethiobiotin
-
Substrates: CO2 in form of HCO3-
Products: -
Products: -
?
ATP + 7,8-diaminononanoate + CO2
ADP + phosphate + dethiobiotin
-
Substrates: -
Products: -
Products: -
?
ATP + 7,8-diaminononanoate + CO2
ADP + phosphate + dethiobiotin
-
Substrates: -
Products: -
Products: -
?
ATP + 7,8-diaminononanoate + CO2
ADP + phosphate + dethiobiotin
-
Substrates: -
Products: -
Products: -
?
ATP + 7,8-diaminononanoate + CO2
ADP + phosphate + dethiobiotin
-
Substrates: -
Products: -
Products: -
?
ATP + 7,8-diaminononanoate + CO2
ADP + phosphate + dethiobiotin
Pseudomonas graveolens
-
Substrates: -
Products: -
Products: -
?
ATP + 7,8-diaminononanoate + CO2
ADP + phosphate + dethiobiotin
-
Substrates: -
Products: -
Products: -
?
ATP + 7,8-diaminononanoate + CO2
ADP + phosphate + dethiobiotin
-
Substrates: -
Products: -
Products: -
?
ATP + 7,8-diaminononanoate + CO2
ADP + phosphate + dethiobiotin
Saccharomyces kloeckerianus
-
Substrates: -
Products: -
Products: -
?
ATP + 7,8-diaminononanoate + CO2
ADP + phosphate + dethiobiotin
-
Substrates: -
Products: -
Products: -
?
ATP + 7,8-diaminononanoate + CO2
ADP + phosphate + dethiobiotin
Sporobolomyces coprophilus
-
Substrates: -
Products: -
Products: -
?
ATP + 7,8-diaminononanoate + CO2
ADP + phosphate + dethiobiotin
-
Substrates: -
Products: -
Products: -
?
ATP + 7,8-diaminononanoate + CO2
ADP + phosphate + dethiobiotin
-
Substrates: -
Products: -
Products: -
?
ATP + diaminobiotin + CO2
ADP + phosphate + biotin
-
Substrates: -
Products: -
Products: -
?
ATP + diaminobiotin + CO2
ADP + phosphate + biotin
-
Substrates: 37% of the activity relative to 7,8-diaminononanoate
Products: -
Products: -
?
ATP + diaminobiotin + CO2
ADP + phosphate + biotin
Pseudomonas graveolens
-
Substrates: -
Products: -
Products: -
?
CTP + (7R,8S)-7,8-diaminopelargonic acid + NaHCO3
CDP + phosphate + dethiobiotin + Na+ + OH-
Substrates: -
Products: -
Products: -
?
CTP + (7R,8S)-7,8-diaminopelargonic acid + NaHCO3
CDP + phosphate + dethiobiotin + Na+ + OH-
Substrates: -
Products: -
Products: -
?
CTP + (7R,8S)-7,8-diaminopelargonic acid + NaHCO3
CDP + phosphate + dethiobiotin + Na+ + OH-
Substrates: -
Products: -
Products: -
?
CTP + 7,8-diaminononanoate + CO2
CDP + phosphate + dethiobiotin
-
Substrates: -
Products: -
Products: -
?
CTP + 7,8-diaminononanoate + CO2
CDP + phosphate + dethiobiotin
-
Substrates: 50% of the activity relative to ATP
Products: -
Products: -
?
CTP + 7,8-diaminononanoate + CO2
CDP + phosphate + dethiobiotin
Pseudomonas graveolens
-
Substrates: -
Products: -
Products: -
?
GTP + (7R,8S)-7,8-diaminopelargonic acid + NaHCO3
GDP + phosphate + dethiobiotin + Na+ + OH-
Substrates: -
Products: -
Products: -
?
GTP + (7R,8S)-7,8-diaminopelargonic acid + NaHCO3
GDP + phosphate + dethiobiotin + Na+ + OH-
Substrates: -
Products: -
Products: -
?
GTP + (7R,8S)-7,8-diaminopelargonic acid + NaHCO3
GDP + phosphate + dethiobiotin + Na+ + OH-
Substrates: -
Products: -
Products: -
?
ITP + (7R,8S)-7,8-diaminopelargonic acid + NaHCO3
IDP + phosphate + dethiobiotin + Na+ + OH-
Substrates: -
Products: -
Products: -
?
ITP + (7R,8S)-7,8-diaminopelargonic acid + NaHCO3
IDP + phosphate + dethiobiotin + Na+ + OH-
Substrates: -
Products: -
Products: -
?
ITP + (7R,8S)-7,8-diaminopelargonic acid + NaHCO3
IDP + phosphate + dethiobiotin + Na+ + OH-
Substrates: -
Products: -
Products: -
?
ITP + 7,8-diaminononanoate + CO2
IDP + phosphate + dethiobiotin
-
Substrates: 8.6% of the activity relative to ATP
Products: -
Products: -
?
ITP + 7,8-diaminononanoate + CO2
IDP + phosphate + dethiobiotin
-
Substrates: 8.6% of the activity relative to ATP
Products: -
Products: -
?
ITP + 7,8-diaminononanoate + CO2
IDP + phosphate + dethiobiotin
Pseudomonas graveolens
-
Substrates: -
Products: -
Products: -
?
TTP + (7R,8S)-7,8-diaminopelargonic acid + NaHCO3
TDP + phosphate + dethiobiotin + Na+ + OH-
Substrates: -
Products: -
Products: -
?
TTP + (7R,8S)-7,8-diaminopelargonic acid + NaHCO3
TDP + phosphate + dethiobiotin + Na+ + OH-
Substrates: -
Products: -
Products: -
?
TTP + (7R,8S)-7,8-diaminopelargonic acid + NaHCO3
TDP + phosphate + dethiobiotin + Na+ + OH-
Substrates: -
Products: -
Products: -
?
UTP + (7R,8S)-7,8-diaminopelargonic acid + NaHCO3
UDP + phosphate + dethiobiotin + Na+ + OH-
Substrates: -
Products: -
Products: -
?
UTP + (7R,8S)-7,8-diaminopelargonic acid + NaHCO3
UDP + phosphate + dethiobiotin + Na+ + OH-
Substrates: -
Products: -
Products: -
?
UTP + 7,8-diaminononanoate + CO2
UDP + phosphate + dethiobiotin
-
Substrates: 7% of the activity relative to ATP
Products: -
Products: -
?
UTP + 7,8-diaminononanoate + CO2
UDP + phosphate + dethiobiotin
-
Substrates: 7% of the activity relative to ATP
Products: -
Products: -
?
UTP + 7,8-diaminononanoate + CO2
UDP + phosphate + dethiobiotin
Pseudomonas graveolens
-
Substrates: -
Products: -
Products: -
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
ATP + 7,8-diaminononanoate + CO2
?
-
Substrates: penultimate enzyme of biotin biosynthesis
Products: -
Products: -
?
ATP + 7,8-diaminononanoate + CO2
ADP + phosphate + dethiobiotin
Substrates: third step in the biosynthesis of biotin, overview
Products: -
Products: -
?
ATP + 7,8-diaminononanoate + CO2
ADP + phosphate + dethiobiotin
-
Substrates: penultimate step in biotin biosynthesis
Products: -
Products: -
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Mg2+
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
(4-[[(1S,2S)-2-(carboxymethyl)cyclopentyl]methyl]phenyl)acetic acid
-
-
-
4-[(1R,2S)-2-(carboxymethyl)cyclopentane-1-carbonyl]benzoic acid
-
-
-
[(1R,2R)-2-[4-(1H-tetrazol-5-yl)benzoyl]cyclopentyl]propanedioic acid
-
-
-
[(1R,2R)-2-[4-(carboxymethyl)benzoyl]cyclopentyl]propanedioic acid
-
-
-
[(1S,2R)-2-(2-hydroxybenzoyl)cyclopentyl]acetic acid
-
lead compound, binds in the 7,8-diaminopelargonic acid pocket. The enantiomer shows higher occupancy than the 1R,2S enantiomer
-
[(1S,2R)-2-[4-(1H-tetrazol-5-yl)benzoyl]cyclopentyl]acetic acid
-
-
-
[(1S,2R)-2-[4-(carboxymethyl)benzoyl]cyclopentyl]acetic acid
-
-
-
ADP
ADP binds in two alternate conformations, both of which extend in the reverse direction compared with the prototypical CTP conformation. In both conformations the ADP beta-phosphate binds at the same position as that observed for CTP, the ADP alpha-phosphate binds at the CTP gamma-phosphate position
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DISEASE
TITLE OF PUBLICATION
LINK TO PUBMED
Tuberculosis
Inhibition of Mycobacterium tuberculosis Dethiobiotin Synthase (MtDTBS): Toward Next-Generation Antituberculosis Agents.
Tuberculosis
Nucleotide triphosphate promiscuity in Mycobacterium tuberculosis dethiobiotin synthetase.
Tuberculosis
Precipitant-ligand exchange technique reveals the ADP binding mode in Mycobacterium tuberculosis dethiobiotin synthetase.
Tuberculosis
Structural characterization of the Mycobacterium tuberculosis biotin biosynthesis enzymes 7,8-diaminopelargonic acid synthase and dethiobiotin synthetase .
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.015
(7R,8S)-7,8-diaminopelargonic acid
mutant G169N, pH 7.5, 37°C
0.03
(7R,8S)-7,8-diaminopelargonic acid
wild-type, pH 7.5, 37°C
0.002
7,8-diaminononanoate
-
pH 7.5, temperature not specified in the publication
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.9
(7R,8S)-7,8-diaminopelargonic acid
mutant G169N, pH 7.5, 37°C
13.3
(7R,8S)-7,8-diaminopelargonic acid
wild-type, pH 7.5, 37°C
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.405
(4-[[(1S,2S)-2-(carboxymethyl)cyclopentyl]methyl]phenyl)acetic acid
-
pH 7.5, 37°C
-
0.367
4-[(1R,2S)-2-(carboxymethyl)cyclopentane-1-carbonyl]benzoic acid
-
pH 7.5, 37°C
-
0.336
[(1R,2R)-2-(2-methoxybenzoyl)cyclopentyl]propanedioic acid
-
pH 7.5, 37°C
-
0.005
[(1R,2R)-2-[4-(1H-tetrazol-5-yl)benzoyl]cyclopentyl]propanedioic acid
-
pH 7.5, 37°C
-
0.356
[(1R,2R)-2-[4-(carboxymethyl)benzoyl]cyclopentyl]propanedioic acid
-
pH 7.5, 37°C
-
0.017
[(1S,2R)-2-[4-(1H-tetrazol-5-yl)benzoyl]cyclopentyl]acetic acid
-
pH 7.5, 37°C
-
0.326
[(1S,2R)-2-[4-(carboxymethyl)benzoyl]cyclopentyl]acetic acid
-
pH 7.5, 37°C
-
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IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
-
-
brenda
active site mutant enzymes: T11V, E12A, E12D, K15Q, K37L, K37Q, K37R, S41A, S41C, overproduced in Escherichia coli strain lacking a functional endogenous DTBS
-
-
brenda
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
BIO3 protein contains an N-terminal sequence that is predicted to target the protein to mitochondria
brenda
Highest Expressing Human Cell Lines
Cell Line LinksPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
metabolism
metabolism
DTBS has two discrete mechanisms to bind NTPs: A high affinity binding mode employed by CTP (KD 160 nM) and a low affinity mode employed by the remaining NTPs (KD > 16.5 microM). Residues Gly12-Val13-Gly14-Lys15 in the P-loop, in combination with Thr16, are a key structural element for both NTP binding modes
metabolism
-
DTBS has two discrete mechanisms to bind NTPs: A high affinity binding mode employed by CTP (KD 160 nM) and a low affinity mode employed by the remaining NTPs (KD > 16.5 microM). Residues Gly12-Val13-Gly14-Lys15 in the P-loop, in combination with Thr16, are a key structural element for both NTP binding modes
-
Show AA Sequence and Transmembrane Helices (12980 entries)
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PDB
SCOP
CATH
UNIPROT
ORGANISM
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
crystallographic studies of complexes with substrates and a reaction intermediate
-
crystals are grown from ammonium sulfate, crystals are soaked in the crystallisation-well solution plus 50 mM 6-hydroxypyrimidin-4(3H)-one for 1 hour, 6-hydroxypyrimidin-4(3H)-one is embedded in the base binding pocket of DTBS
-
hanging-drop vapor diffusion, 0.005 ml of well solution containing 100 mM magnesium acetate or MgCl2, 9-11% polyethylene glycol 8000 and 100 mM cacodylate, pH 6.5 are mixed with 0.002 ml protein solution containing 30 mg/ml DTBS, crystals grow within a week at 20°C, crystals of DTBS complexed with diaminopelargonic acid-MgADP-AlF3 and with dethiobiotin-MgADP-phosphate, crystals diffract to 1.8 A
-
hanging-drop vapor diffusion, precipitant polyethylene glycol 8000, 100 mM cacodylate, pH 6.5, 200 mM magnesium acetate, crystals diffract to 0.97 A
-
in complex with CTP, to 2.3 A resolution. The nucleoside base is stabilized in its pocket through hydrogen-bonding interactions with the protein backbone, rather than amino acid side chains. DTBS could utilise ATP, CTP, GTP, ITP, TTP, or UTP with similar Km and kcat values
X-ray crystallographic studies of the mutant enzymes S41A, S41C, K37Q, and K37L, show that the crystals are essentially isomorphous to that of the wild-type DTBS
-
in complex with CTP, to 2.3 A resolution. The nucleoside base is stabilized in its pocket through hydrogen-bonding interactions with the protein backbone, rather than amino acid side chains. DTBS could utilise ATP, CTP, GTP, ITP, TTP, or UTP with similar Km and kcat values
in complexes with the substrate 7,8-diaminopelargonic acid or ADP and the product dethiobiotin, up to 1.85 A resolution.
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
T11V
-
active site mutant enzymes: T11V, E12A, E12D, K15Q, K37L, K37Q, K37R, S41A, S41C, T11V mutant shows a 24000fold increase in the Km for ATP with little or no change in the Km for 7,8-diaminononanoate and in turnover number. Mutants E12A and E12D show wild-type activity with slightly elevated turnover numbers. Unlike wild-type enzyme mutant enzyme E12A has the same apparent Km at subsaturating and saturating ATP concentrations. Mutant enzymes K15Q, K37Q, and K37R have no catalytic activity. Mutant enzymes S41A and S41C have the same turnover number as the wild-type enzyme and a moderate increase in Km for ATP and 7,8-diaminononanoate
G169N
additional information
construction of bio3 insertion mutants, which have a similar phenotype to the bio1 and bio2 auxotrophs identified using forward genetic screens for arrested embryos rescued on enriched nutrient medium. Genes bio3 and bio1 mutants define a single genetic complementation group, separate BIO3 and BIO1 transcripts and two different types of chimeric BIO3-BIO1 transcripts are produced. One of the fused transcripts is monocistronic and encodes a bifunctional fusion protein. A splice variant is bicistronic, with distinct but overlapping reading frames. Dual functionality of the monocistronic transcript is confirmed by complementing the orthologous auxotrophs of Escherichia coli strain. Allelism between bio1 and bio3 heterozygotes and phenotypes, overview
G169N
Km value for (7R, 8S)-7,8-diaminopelargonic acid similar to wild-type, 3fold increase in Km value for carbonate
G169N
-
Km value for (7R, 8S)-7,8-diaminopelargonic acid similar to wild-type, 3fold increase in Km value for carbonate
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
active site mutant enzymes: T11V, E12A, E12D, K15Q, K37L, K37Q, K37R, S41A, S41C, overproduced in Escherichia coli
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
gene bio3, alleles bio1-3, bio2-3, and bio3-3, DNA and amino acid sequence determination and analysis and genotyping, encoded with gene bio1 in a bifunctional locus that catalyzes two sequential reactions in the same metabolic pathway via differential splicing, separate BIO3 and BIO1 transcripts and two different types of chimeric BIO3-BIO1 transcripts are produced. One of the fused transcripts is monocistronic and encodes a bifunctional fusion protein. A splice variant is bicistronic, with distinct but overlapping reading frames, overview
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
analysis
analysis
development of a crystallographic soaking technique for precipitant-ligand exchange to exchange protein-bound precipitants with ligands of interest
analysis
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development of a crystallographic soaking technique for precipitant-ligand exchange to exchange protein-bound precipitants with ligands of interest
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REF.
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59
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brenda
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brenda
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Structure
2
407-414
1994
Escherichia coli
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759-760
1994
Escherichia coli
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559-560
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Escherichia coli
-
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Active site mutants of the Escherichia coli dethiobiotin synthetase: effects of mutations on enzyme catalytic and structural properties
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36
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DNA Seq.
4
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[Brevibacterium] flavum
brenda
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Cloning and characterization of the Bacillus sphaericus genes controlling the bioconversion of pimelate into dethiobiotin
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87
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Mechanism of an ATP-dependent carboxylase, dethiobiotin synthetase, based on crystallographic studies of complexes with substrates and a reaction intermediate
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34
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Structure of dethiobiotin synthetase at 0.97 A resolution
Acta Crystallogr. Sect. D
55
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Escherichia coli
-
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Kack, H.; Sandmark, J.; Gibson, K.J.; Schneider, G.; Lindqvist, Y.
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-
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Muralla, R.; Chen, E.; Sweeney, C.; Gray, J.A.; Dickerman, A.; Nikolau, B.J.; Meinke, D.
A bifunctional locus (BIO3-BIO1) required for biotin biosynthesis in Arabidopsis
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Arabidopsis thaliana (B0F481)
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Structural characterization of the Mycobacterium tuberculosis biotin biosynthesis enzymes 7,8-diaminopelargonic acid synthase and dethiobiotin synthetase
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Mycobacterium tuberculosis
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8
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Mycobacterium tuberculosis (P9WPQ5), Mycobacterium tuberculosis H37Rv (P9WPQ5)
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Mycobacterium tuberculosis (P9WPQ5), Mycobacterium tuberculosis H37Rv (P9WPQ5)
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