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Information on EC 2.3.1.117 - 2,3,4,5-tetrahydropyridine-2,6-dicarboxylate N-succinyltransferase and Organism(s) Mycobacterium tuberculosis and UniProt Accession P9WP21

for references in articles please use BRENDA:EC2.3.1.117
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EC Tree
IUBMB Comments
Involved in the biosynthesis of lysine in bacteria (including cyanobacteria) and higher plants. The 1992 edition of the Enzyme List erroneously gave the name 2,3,4,5-tetrahydropyridine-2-carboxylate N-succinyltransferase to this enzyme.
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This record set is specific for:
Mycobacterium tuberculosis
UNIPROT: P9WP21
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Word Map
The taxonomic range for the selected organisms is: Mycobacterium tuberculosis
The expected taxonomic range for this enzyme is: Bacteria, Archaea, Eukaryota
Synonyms
tetrahydrodipicolinate n-succinyltransferase, tetrahydrodipicolinate succinylase, mtb-dapd, tetrahydrodipicolinate-n-succinyltransferase, succinyl-coa:tetrahydrodipicolinate n-succinyltransferase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Mtb-DapD
in complex with cofactor succinyl-CoA
tetrahydrodipicolinate N-succinyltransferase
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succinyl-CoA:tetrahydrodipicolinate N-succinyltransferase
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succinyltransferase, tetrahydrodipicolinate
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tetrahydrodipicolinate N-succinyltransferase
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tetrahydrodipicolinate succinylase
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tetrahydrodipicolinate succinyltransferase
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tetrahydrodipicolinate-N-succinyltransferase
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Acyl group transfer
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SYSTEMATIC NAME
IUBMB Comments
succinyl-CoA:(S)-2,3,4,5-tetrahydropyridine-2,6-dicarboxylate N-succinyltransferase
Involved in the biosynthesis of lysine in bacteria (including cyanobacteria) and higher plants. The 1992 edition of the Enzyme List erroneously gave the name 2,3,4,5-tetrahydropyridine-2-carboxylate N-succinyltransferase to this enzyme.
CAS REGISTRY NUMBER
COMMENTARY hide
88086-34-4
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Ca2+
slight increase of enzyme activity
Mg2+
stabilizes quartenary enzyme structure, slight increase of enzyme activity
Mn2+
slight increase of enzyme activity
Na+
stabilizes quartenary enzyme structure
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
acetate
caused by inhibition of succinyl-CoA-binding or pH effect
Co2+
partial inhibition
Zn2+
1 mM, complete loss of enzyme acitivity
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
part of L-lysine biosynthetic pathway
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
100000
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gel filtration, homotrimer
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
homotrimer
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gel filtration
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
crystallized in the cubic space group I23 or I213. Diffraction data analysis indicates the presence of five molecules per asymmetric unit. Data exhibit icosahedral point-group symmetry. Enzyme might assembles into a 60-mer exhibiting 235 point-group symmetry and crystallizes as such in space group I23. In this case, the combination of crystallographic and noncrystallographic symmetry elements results in an arrangement of the icosahedrons in the cubic crystal with one pentamer in the asymmetric unit. Another explanation is that the packing of the molecules itself mimics icosahedral symmetry. In this case both space groups I23 and I213 would be possible
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
E199A
completely inactive mutant
G222P
completely inactive mutant
additional information
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
affinity and size-exclusion chromatography
using affinity chromatography and gel filtration
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
expressed in Escherichia coli
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Schuldt, L.; Weyand, S.; Kefala, G.; Weiss, M.S.
Cloning, expression, purification, crystallization and preliminary X-ray diffraction analysis of tetrahydrodipicolinate-N-succinyltransferase (Rv1201c) from Mycobacterium tuberculosis
Acta Crystallogr. Sect. F
64
863-866
2008
Mycobacterium tuberculosis
Manually annotated by BRENDA team
Schuldt, L.; Weyand, S.; Kefala, G.; Weiss, M.S.
The three-dimensional Structure of a mycobacterial DapD provides insights into DapD diversity and reveals unexpected particulars about the enzymatic mechanism
J. Mol. Biol.
389
863-879
2009
Mycobacterium tuberculosis (P9WP21), Mycobacterium tuberculosis
Manually annotated by BRENDA team