BRENDA - Enzyme Database show
show all sequences of 2.6.1.62

Inhibition of 7,8-diaminopelargonic acid aminotransferase from Mycobacterium tuberculosis by chiral and achiral anologs of its substrate: biological implications

Mann, S.; Colliandre, L.; Labesse, G.; Ploux, O.; Biochimie 91, 826-834 (2009)

Data extracted from this reference:

Application
Application
Commentary
Organism
analysis
analytical method to measure the enantiomeric excess of substrate 8-amino-7-oxononanoic acid, based on the derivatization of its amine function, by orthophtalaldehyde and N-acetyl-L-cysteine, followed by high pressure liquid chromatography separation. Using this methodology and enantiopure samples of 8-amino-7-oxononanoic acid, it appears that racemization of 8-amino-7-oxononanoic acid occurs rapidly with half-lives from 1 to 8 h, not only in 4 M HCl but also in the usual pH range, from 7 to 9
Mycobacterium tuberculosis
Inhibitors
Inhibitors
Commentary
Organism
Structure
(R)-8-amino-7-oxononanoate
binds both to the pyridoxal 5'-phosphate form and to the pyridoxamine 5'-phosphate form by forming specific hydrogen bonds with residue T309 and the phosphate group of the cofactor
Mycobacterium tuberculosis
(R)-8-amino-7-oxononanoic acid
potent inhibitor
Mycobacterium tuberculosis
8-amino-7-oxooctanoate
potent inhibitor
Mycobacterium tuberculosis
8-amino-7-oxooctanoic acid
achiral analog of 8-amino-7-oxononanoate
Mycobacterium tuberculosis
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Mycobacterium tuberculosis
-
-
-
Mycobacterium tuberculosis
P9WQ81
-
-
Mycobacterium tuberculosis ATCC 25618
P9WQ81
-
-
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
S-adenosyl-L-methionine + (S)-8-amino-7-oxononanoate
enzyme only uses (S)-8-amino-7-oxononanoate as substrate
702483
Mycobacterium tuberculosis
S-adenosyl-4-methylthio-2-oxobutanoate + 7,8-diaminononanoate
-
-
-
?
S-adenosyl-L-methionine + (S)-8-amino-7-oxononanoate
enzyme only uses (S)-8-amino-7-oxononanoate as substrate
702483
Mycobacterium tuberculosis ATCC 25618
S-adenosyl-4-methylthio-2-oxobutanoate + 7,8-diaminononanoate
-
-
-
?
S-adenosyl-L-methionine + (S)-8-amino-7-oxononanoic acid
-
702483
Mycobacterium tuberculosis
S-adenosyl-4-methylthio-2-oxobutanoate + (7S,8R)-diaminononanoate
-
-
-
?
Cofactor
Cofactor
Commentary
Organism
Structure
pyridoxal 5'-phosphate
-
Mycobacterium tuberculosis
pyridoxamine 5'-phosphate
-
Mycobacterium tuberculosis
Ki Value [mM]
Ki Value [mM]
Ki Value maximum [mM]
Inhibitor
Commentary
Organism
Structure
0.0009
-
8-amino-7-oxooctanoate
bound to the pyridoxamine 5'-phosphate form, 100 mM EPPS buffer, pH 8.6
Mycobacterium tuberculosis
0.0009
-
8-amino-7-oxooctanoic acid
binding to the the pyridoxamine 5'-phosphate form of enzyme, pH not specified in the publication, temperature not specified in the publication
Mycobacterium tuberculosis
0.0017
-
(R)-8-amino-7-oxononanoate
binding to the the pyridoxamine 5'-phosphate form of enzyme, pH not specified in the publication, temperature not specified in the publication
Mycobacterium tuberculosis
0.0017
-
(R)-8-amino-7-oxononanoic acid
bound to the pyridoxamine 5'-phosphate form, 100 mM EPPS buffer, pH 8.6
Mycobacterium tuberculosis
0.0042
-
8-amino-7-oxooctanoate
bound to the pyridoxal 5'-phosphate form, 100 mM EPPS buffer, pH 8.6
Mycobacterium tuberculosis
0.0042
-
8-amino-7-oxooctanoic acid
binding to the the pyridoxal 5'-phosphate form of enzyme, pH not specified in the publication, temperature not specified in the publication
Mycobacterium tuberculosis
0.0059
-
(R)-8-amino-7-oxononanoate
binding to the the pyridoxal 5'-phosphate form of enzyme, pH not specified in the publication, temperature not specified in the publication
Mycobacterium tuberculosis
0.0059
-
(R)-8-amino-7-oxononanoic acid
bound to the pyridoxal 5'-phosphate enzyme form, 100 mM EPPS buffer, pH 8.6
Mycobacterium tuberculosis
Application (protein specific)
Application
Commentary
Organism
analysis
analytical method to measure the enantiomeric excess of substrate 8-amino-7-oxononanoic acid, based on the derivatization of its amine function, by orthophtalaldehyde and N-acetyl-L-cysteine, followed by high pressure liquid chromatography separation. Using this methodology and enantiopure samples of 8-amino-7-oxononanoic acid, it appears that racemization of 8-amino-7-oxononanoic acid occurs rapidly with half-lives from 1 to 8 h, not only in 4 M HCl but also in the usual pH range, from 7 to 9
Mycobacterium tuberculosis
Cofactor (protein specific)
Cofactor
Commentary
Organism
Structure
pyridoxal 5'-phosphate
-
Mycobacterium tuberculosis
pyridoxamine 5'-phosphate
-
Mycobacterium tuberculosis
Inhibitors (protein specific)
Inhibitors
Commentary
Organism
Structure
(R)-8-amino-7-oxononanoate
binds both to the pyridoxal 5'-phosphate form and to the pyridoxamine 5'-phosphate form by forming specific hydrogen bonds with residue T309 and the phosphate group of the cofactor
Mycobacterium tuberculosis
(R)-8-amino-7-oxononanoic acid
potent inhibitor
Mycobacterium tuberculosis
8-amino-7-oxooctanoate
potent inhibitor
Mycobacterium tuberculosis
8-amino-7-oxooctanoic acid
achiral analog of 8-amino-7-oxononanoate
Mycobacterium tuberculosis
Ki Value [mM] (protein specific)
Ki Value [mM]
Ki Value maximum [mM]
Inhibitor
Commentary
Organism
Structure
0.0009
-
8-amino-7-oxooctanoate
bound to the pyridoxamine 5'-phosphate form, 100 mM EPPS buffer, pH 8.6
Mycobacterium tuberculosis
0.0009
-
8-amino-7-oxooctanoic acid
binding to the the pyridoxamine 5'-phosphate form of enzyme, pH not specified in the publication, temperature not specified in the publication
Mycobacterium tuberculosis
0.0017
-
(R)-8-amino-7-oxononanoate
binding to the the pyridoxamine 5'-phosphate form of enzyme, pH not specified in the publication, temperature not specified in the publication
Mycobacterium tuberculosis
0.0017
-
(R)-8-amino-7-oxononanoic acid
bound to the pyridoxamine 5'-phosphate form, 100 mM EPPS buffer, pH 8.6
Mycobacterium tuberculosis
0.0042
-
8-amino-7-oxooctanoate
bound to the pyridoxal 5'-phosphate form, 100 mM EPPS buffer, pH 8.6
Mycobacterium tuberculosis
0.0042
-
8-amino-7-oxooctanoic acid
binding to the the pyridoxal 5'-phosphate form of enzyme, pH not specified in the publication, temperature not specified in the publication
Mycobacterium tuberculosis
0.0059
-
(R)-8-amino-7-oxononanoate
binding to the the pyridoxal 5'-phosphate form of enzyme, pH not specified in the publication, temperature not specified in the publication
Mycobacterium tuberculosis
0.0059
-
(R)-8-amino-7-oxononanoic acid
bound to the pyridoxal 5'-phosphate enzyme form, 100 mM EPPS buffer, pH 8.6
Mycobacterium tuberculosis
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
S-adenosyl-L-methionine + (S)-8-amino-7-oxononanoate
enzyme only uses (S)-8-amino-7-oxononanoate as substrate
702483
Mycobacterium tuberculosis
S-adenosyl-4-methylthio-2-oxobutanoate + 7,8-diaminononanoate
-
-
-
?
S-adenosyl-L-methionine + (S)-8-amino-7-oxononanoate
enzyme only uses (S)-8-amino-7-oxononanoate as substrate
702483
Mycobacterium tuberculosis ATCC 25618
S-adenosyl-4-methylthio-2-oxobutanoate + 7,8-diaminononanoate
-
-
-
?
S-adenosyl-L-methionine + (S)-8-amino-7-oxononanoic acid
-
702483
Mycobacterium tuberculosis
S-adenosyl-4-methylthio-2-oxobutanoate + (7S,8R)-diaminononanoate
-
-
-
?
Other publictions for EC 2.6.1.62
No.
1st author
Pub Med
title
organims
journal
volume
pages
year
Activating Compound
Application
Cloned(Commentary)
Crystallization (Commentary)
Engineering
General Stability
Inhibitors
KM Value [mM]
Localization
Metals/Ions
Molecular Weight [Da]
Natural Substrates/ Products (Substrates)
Organic Solvent Stability
Organism
Oxidation Stability
Posttranslational Modification
Purification (Commentary)
Reaction
Renatured (Commentary)
Source Tissue
Specific Activity [micromol/min/mg]
Storage Stability
Substrates and Products (Substrate)
Subunits
Temperature Optimum [°C]
Temperature Range [°C]
Temperature Stability [°C]
Turnover Number [1/s]
pH Optimum
pH Range
pH Stability
Cofactor
Ki Value [mM]
pI Value
IC50 Value
Activating Compound (protein specific)
Application (protein specific)
Cloned(Commentary) (protein specific)
Cofactor (protein specific)
Crystallization (Commentary) (protein specific)
Engineering (protein specific)
General Stability (protein specific)
IC50 Value (protein specific)
Inhibitors (protein specific)
Ki Value [mM] (protein specific)
KM Value [mM] (protein specific)
Localization (protein specific)
Metals/Ions (protein specific)
Molecular Weight [Da] (protein specific)
Natural Substrates/ Products (Substrates) (protein specific)
Organic Solvent Stability (protein specific)
Oxidation Stability (protein specific)
Posttranslational Modification (protein specific)
Purification (Commentary) (protein specific)
Renatured (Commentary) (protein specific)
Source Tissue (protein specific)
Specific Activity [micromol/min/mg] (protein specific)
Storage Stability (protein specific)
Substrates and Products (Substrate) (protein specific)
Subunits (protein specific)
Temperature Optimum [°C] (protein specific)
Temperature Range [°C] (protein specific)
Temperature Stability [°C] (protein specific)
Turnover Number [1/s] (protein specific)
pH Optimum (protein specific)
pH Range (protein specific)
pH Stability (protein specific)
pI Value (protein specific)
Expression
General Information
General Information (protein specific)
Expression (protein specific)
KCat/KM [mM/s]
KCat/KM [mM/s] (protein specific)
738841
Dai
Fragment-based exploration of ...
Mycobacterium tuberculosis, Mycobacterium tuberculosis H37Rv
J. Med. Chem.
58
5208-5217
2015
-
-
-
1
-
-
3
-
-
-
-
-
-
3
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
3
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
738054
Dai
Inhibition of Mycobacterium tu ...
Mycobacterium tuberculosis, Mycobacterium tuberculosis H37Rv
ChemBioChem
15
575-586
2014
-
-
-
1
-
-
2
-
-
-
-
-
-
4
-
-
-
-
-
-
-
-
-
-
-
-
2
-
-
-
-
-
1
-
-
-
-
-
-
1
-
-
-
2
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
2
-
-
-
-
-
-
-
-
-
-
-
721279
Mann
A microplate fluorescence assa ...
Mycobacterium tuberculosis, Mycobacterium tuberculosis ATCC 25618
Anal. Biochem.
432
90-96
2013
-
1
-
-
-
-
2
-
-
-
-
-
-
7
-
-
-
-
-
-
-
-
2
-
-
-
-
-
-
-
-
-
2
-
-
-
2
-
-
-
-
-
-
3
2
-
-
-
-
-
-
-
-
-
-
-
-
-
2
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
723412
Cobessi
Biochemical and structural cha ...
Arabidopsis thaliana
Plant Cell
24
1608-1625
2012
-
1
1
1
3
-
-
6
1
-
1
1
-
7
-
-
-
-
-
-
-
-
5
2
-
-
-
2
-
-
-
-
-
-
-
-
1
1
-
1
3
-
-
-
-
6
1
-
1
1
-
-
-
-
-
-
-
-
5
2
-
-
-
2
-
-
-
-
-
-
-
-
-
-
728182
Shi
Design and synthesis of potent ...
Mycobacterium tuberculosis, Mycobacterium tuberculosis ATCC 25618
J. Org. Chem.
77
6051-6058
2012
-
-
-
-
-
-
1
-
-
-
-
-
-
5
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
1
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
714208
Dey
Structural characterization of ...
Mycobacterium tuberculosis, Mycobacterium tuberculosis CDC 1551
Biochemistry
49
6746-6760
2010
-
-
1
1
-
-
-
2
-
-
-
-
-
7
-
-
-
-
-
-
-
-
4
-
-
-
-
2
-
-
-
1
-
-
-
-
-
1
1
1
-
-
-
-
-
2
-
-
-
-
-
-
-
-
-
-
-
-
4
-
-
-
-
2
-
-
-
-
-
-
-
-
2
2
702483
Mann
Inhibition of 7,8-diaminopelar ...
Mycobacterium tuberculosis, Mycobacterium tuberculosis ATCC 25618
Biochimie
91
826-834
2009
-
1
-
-
-
-
4
-
-
-
-
-
-
6
-
-
-
-
-
-
-
-
3
-
-
-
-
-
-
-
-
2
8
-
-
-
1
-
2
-
-
-
-
4
8
-
-
-
-
-
-
-
-
-
-
-
-
-
3
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
673564
Mann
7,8-Diaminoperlargonic acid am ...
Mycobacterium tuberculosis, Mycobacterium tuberculosis ATCC 25618
FEBS J.
273
4778-4789
2006
-
-
1
-
-
-
3
2
-
-
2
-
-
8
-
-
1
1
-
-
-
-
3
1
-
-
-
2
-
-
-
1
4
-
-
-
-
1
1
-
-
-
-
6
6
4
-
-
2
-
-
-
-
1
-
-
-
-
3
1
-
-
-
2
-
-
-
-
-
-
-
-
-
-
661047
Mann
Inhibition of 7,8-diaminopelar ...
Escherichia coli, Mycobacterium tuberculosis
Biochem. Soc. Trans.
33
802-805
2005
-
1
1
-
-
-
3
3
-
-
-
2
-
2
-
-
1
1
-
-
-
-
4
-
-
-
-
2
-
-
-
2
3
-
-
-
1
1
2
-
-
-
-
3
3
3
-
-
-
2
-
-
-
1
-
-
-
-
4
-
-
-
-
2
-
-
-
-
-
-
-
-
-
-
661370
Van Arsdell
Removing a bottleneck in the B ...
Bacillus subtilis
Biotechnol. Bioeng.
91
75-83
2005
-
1
1
-
-
-
1
1
-
-
-
1
-
5
-
-
-
1
-
-
1
-
3
-
1
-
-
-
1
-
-
1
-
-
-
-
1
1
1
-
-
-
-
1
-
1
-
-
-
1
-
-
-
-
-
-
1
-
3
-
1
-
-
-
1
-
-
-
-
-
-
-
-
-
661088
Sandmark
Conserved and nonconserved res ...
Escherichia coli
Biochemistry
43
1213-1222
2004
-
-
1
1
7
-
-
16
-
-
-
1
-
2
-
-
-
1
-
-
-
-
3
-
-
-
-
15
1
-
-
1
-
-
-
-
-
1
1
1
7
-
-
-
-
16
-
-
-
1
-
-
-
-
-
-
-
-
3
-
-
-
-
15
1
-
-
-
-
-
-
-
-
-
660565
Eliot
Avoiding the road less travele ...
Escherichia coli
Acc. Chem. Res.
36
757-765
2003
-
-
-
-
-
-
1
1
-
-
-
1
-
1
-
-
-
1
-
-
-
-
2
-
-
-
-
2
-
-
-
1
-
-
-
-
-
-
1
-
-
-
-
1
-
1
-
-
-
1
-
-
-
-
-
-
-
-
2
-
-
-
-
2
-
-
-
-
-
-
-
-
-
-
663002
Breen
The mechanism of 7,8-diaminope ...
Escherichia coli
Org. Biomol. Chem.
1
3498-3499
2003
-
-
1
-
-
-
1
1
-
-
-
1
-
1
-
-
1
1
-
-
-
-
2
-
-
-
-
-
1
-
-
1
-
-
-
-
-
1
1
-
-
-
-
1
-
1
-
-
-
1
-
-
-
1
-
-
-
-
2
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
637095
Eliot
The dual-specific active site ...
Escherichia coli
Biochemistry
41
12582-12589
2002
-
-
1
1
1
-
1
3
-
-
-
1
-
1
-
-
-
-
-
-
-
-
2
-
-
-
-
2
-
-
-
-
1
-
-
-
-
1
-
1
1
-
-
1
1
3
-
-
-
1
-
-
-
-
-
-
-
-
2
-
-
-
-
2
-
-
-
-
-
-
-
-
-
-
637097
Käck
Crystal structure of diaminope ...
Escherichia coli
J. Mol. Biol.
291
857-876
1999
-
-
-
1
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
1
-
-
-
-
-
-
1
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
637096
Käck
Purification and preliminary x ...
Escherichia coli
Acta Crystallogr. Sect. D
54
1397-1398
1998
-
-
1
1
-
-
-
-
-
-
-
-
-
2
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1335
Izumi
Microbiological biosynthesis o ...
Bacillus roseus, Bacillus roseus IAM 1257, Corynebacterium glutamicum, Kocuria rosea, Salmonella enterica subsp. enterica serovar Typhimurium
Methods Enzymol.
62
326-338
1979
-
-
-
-
-
-
9
-
-
-
-
5
-
7
-
-
1
-
-
-
1
-
11
-
1
-
1
-
1
-
1
8
-
-
-
-
-
-
8
-
-
-
-
9
-
-
-
-
-
5
-
-
-
1
-
-
1
-
11
-
1
-
1
-
1
-
1
-
-
-
-
-
-
-
637094
Eisenberg
7,8-Diaminopelargonic acid ami ...
Escherichia coli
Methods Enzymol.
62
342-347
1979
-
-
-
-
-
-
5
5
-
-
2
-
-
1
-
-
1
-
-
-
1
1
3
1
-
-
-
1
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
5
1
5
-
-
2
-
-
-
-
1
-
-
1
1
3
1
-
-
-
1
-
-
-
-
-
-
-
-
-
-
637089
Stoner
Purification and properties of ...
Escherichia coli
J. Biol. Chem.
250
4029-4036
1975
-
-
-
-
-
-
-
-
-
-
2
-
-
1
-
-
1
-
-
-
1
-
7
1
-
-
-
-
-
-
-
1
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
2
-
-
-
-
1
-
-
1
-
7
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
637090
Izumi
-
Biosynthesis of biotin by micr ...
Bacillus roseus, Bacillus roseus IAM 1257, Corynebacterium glutamicum, Corynebacterium glutamicum NRRL 2311, Escherichia coli, Escherichia coli AKV 0015, Kocuria rosea, Salmonella enterica subsp. enterica serovar Typhimurium
Agric. Biol. Chem.
39
175-181
1975
-
-
-
-
-
-
16
5
-
-
1
8
-
11
-
-
1
-
-
-
-
-
20
-
2
1
2
-
2
-
1
10
-
-
-
-
-
-
10
-
-
-
-
16
-
5
-
-
1
8
-
-
-
1
-
-
-
-
20
-
2
1
2
-
2
-
1
-
-
-
-
-
-
-
637092
Stoner
Biosynthesis of 7,8-diaminopel ...
Corynebacterium glutamicum, Corynebacterium glutamicum NRRL 2311, Escherichia coli
J. Biol. Chem.
250
4037-4043
1975
-
-
-
-
-
-
9
4
-
-
-
-
-
4
-
-
-
1
-
-
2
-
6
-
2
-
-
1
2
-
-
4
1
-
-
-
-
-
4
-
-
-
-
9
1
4
-
-
-
-
-
-
-
-
-
-
2
-
6
-
2
-
-
1
2
-
-
-
-
-
-
-
-
-
637091
Izumi
-
7,8-Diaminopelargonic acid ami ...
Bacillus roseus, Bacillus roseus IAM 1257, Corynebacterium glutamicum, Escherichia coli, Kocuria rosea, Salmonella enterica subsp. enterica serovar Typhimurium
Agric. Biol. Chem.
37
2683-2684
1973
-
-
-
-
-
-
-
-
-
-
-
6
-
8
-
-
1
-
-
-
3
-
12
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
6
-
-
-
1
-
-
3
-
12
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-