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Information on EC 1.2.1.11 - aspartate-semialdehyde dehydrogenase and Organism(s) Mycobacterium tuberculosis and UniProt Accession P9WNX5

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Mycobacterium tuberculosis
UNIPROT: P9WNX5 not found.
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The taxonomic range for the selected organisms is: Mycobacterium tuberculosis
The enzyme appears in selected viruses and cellular organisms
Synonyms
asadh, aspartate semialdehyde dehydrogenase, aspartate-beta-semialdehyde dehydrogenase, aspartate-semialdehyde dehydrogenase, aspartate beta-semialdehyde dehydrogenase, asa dh, aspartic semialdehyde dehydrogenase, l-aspartate-beta-semialdehyde dehydrogenase, asd enzyme, ecasadh, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
aspartate semialdehyde dehydrogenase
-
aspartate-beta-semialdehyde dehydrogenase
-
aspartate-beta-semialdeyhyde dehydrogenase
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aspartyl beta-semialdehyde dehydrogenase
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ASA dehydrogenase
-
-
-
-
ASA DH
-
-
-
-
ASADH
aspartate semialdehyde dehydrogenase
aspartic acid semialdehyde dehydrogenase
-
-
aspartic beta-semialdehyde dehydrogenase
-
-
-
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aspartic semialdehyde dehydrogenase
-
-
-
-
dehydrogenase, aspartate semialdehyde
-
-
-
-
L-aspartate-beta-semialdehyde:NADP oxidoreductase (phosphorylating)
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Phosphorylation
-
-
-
-
redox reaction
-
-
-
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oxidation
-
-
-
-
reduction
-
-
-
-
SYSTEMATIC NAME
IUBMB Comments
L-aspartate-4-semialdehyde:NADP+ oxidoreductase (phosphorylating)
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CAS REGISTRY NUMBER
COMMENTARY hide
9000-98-0
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
aspartate-4-semialdehyde + phosphate + NADP+
L-4-aspartyl phosphate + NADPH + H+
show the reaction diagram
second enzyme in the lysine/homoserine biosynthetic pathways
-
-
r
L-4-aspartyl phosphate + NADPH
L-aspartate-4-semialdehyde + phosphate + NADP+
show the reaction diagram
physiological forward reaction direction, key enzyme in diaminopimelic acid biosynthetic pathway
-
-
?
L-4-aspartyl phosphate + NADPH + H+
L-aspartate 4-semialdehyde + phosphate + NADP+
show the reaction diagram
-
-
-
?
L-aspartate 4-semialdehyde + phosphate + NADP+
L-4-aspartyl phosphate + NADPH + H+
show the reaction diagram
L-aspartate-4-semialdehyde + phosphate + NADP+
L-4-aspartyl phosphate + NADPH
show the reaction diagram
-
-
-
r
L-aspartate 4-semialdehyde + phosphate + NADP+
L-4-aspartyl phosphate + NADPH + H+
show the reaction diagram
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
aspartate-4-semialdehyde + phosphate + NADP+
L-4-aspartyl phosphate + NADPH + H+
show the reaction diagram
second enzyme in the lysine/homoserine biosynthetic pathways
-
-
r
L-4-aspartyl phosphate + NADPH
L-aspartate-4-semialdehyde + phosphate + NADP+
show the reaction diagram
physiological forward reaction direction, key enzyme in diaminopimelic acid biosynthetic pathway
-
-
?
L-4-aspartyl phosphate + NADPH + H+
L-aspartate 4-semialdehyde + phosphate + NADP+
show the reaction diagram
-
-
-
?
L-aspartate 4-semialdehyde + phosphate + NADP+
L-4-aspartyl phosphate + NADPH + H+
show the reaction diagram
L-aspartate 4-semialdehyde + phosphate + NADP+
L-4-aspartyl phosphate + NADPH + H+
show the reaction diagram
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
NADP+
NADP+
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
molecular docking and simulation studies of the priority target, enzyme ASD, reveals the therapeutic potential of the ASD inhibitors based on selected natural products (huperzine A, rosmarinic acid, and curcumin), overview
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.955
L-aspartate-4-semialdehyde
recombinant enzyme, pH 9.0, 30°C
0.065
NADP+
recombinant enzyme, pH 9.0, 30°C
11.39
phosphate
recombinant enzyme, pH 9.0, 30°C
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
8.49
NADP+
recombinant enzyme, pH 9.0, 30°C
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
metabolism
malfunction
-
enzyme deficiency or inhibition of enzyme activity leads to 80% reduced cell wall materials compared to the wild-type, in addition to obvious morphological differences, phenotype, overview
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
37000
x * 37000, about, recombinant enzyme, SDS-PAGE
38070
the expressed and purified monomer protein construct includes the 17-amino-acid sequence RGSHHHHHHGSACELGT between the N-terminal Met and the second amino acid Gly of the native Asd sequence, the total length of this protein is 362 amino acids
75000
homodimer in solution, determined by gel filtration
37000
2 * 37000, about, recombinant His-tagged enzyme, SDS-PAGE
75000
recombinant His-tagged enzyme, gel filtration
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
x * 37000, about, recombinant enzyme, SDS-PAGE
dimer
dimerization domain structure, overview
homodimer
recombinant enzyme
dimer
2 * 37000, about, recombinant His-tagged enzyme, SDS-PAGE
additional information
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
by using the hanging-drop vapour-diffusion method, crystallization in 2 different crystal forms, diffraction data analysis suggests the presence of up to four monomers in the asymmetric unit of the orthorhombic crystal form and of one or 2 monomers in the cubic crystal form
in complex with S-methyl-l-cysteine sulfoxide and sulfate, sitting drop vapor diffusion method, using 1.6 M ammonium sulfate and 100 mM citric acid pH 5.0
purified recombinant His-tagged enzyme, 9 mg/ml protein in 10 mM potassium phosphate buffer, pH 8.0, and 10 mM DTT, sitting drop vapour diffusion method, mixing of 500 nl of protein and of reservoir solution, the latter containing 1.6 M ammonium sulfate and 100 mM citric acid, pH 5.0, 2 days at 18°C, two different crystal forms, X-ray diffraction structure determination and analysis at 2.18-2.75 A resolution
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
-
construction of an gene asadh promoter-replacement mutant Mycobacterium tuberculosis strain, designated MTB::asadh, in which the asadh gene expression is regulated by pristinamycin. Bacterial growth is survival of MTB::asadh in host cells is completely inhibited in the absence of the inducer pristinamycin. The growth of the mutant is rigorously dependent on the presence of the inducer in the medium. The starved mutant exhibits a marked reduction (approximately 80%) in the cell wall materials compared to the wild-type, in addition to obvious morphological differences, phenotype, overview. With the addition of pristinamycin, the cell wall contents and morphology are recovered in a similar manner to those of the wild-type strain. The starved mutant also exhibits almost no pathogenicity in an in vitro model of infection using mouse macrophage J774A.1 cells. The mutant shows a concentration-dependent recovery of pathogenicity with the addition of the inducer
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
by using affinity chromatography and gel filtration
Ni-NTA column chromatography and gel filtration
recombinant His-tagged enzyme from Escherichia coli by nickel affinity chromatography to 96% purity
recombinant His-tagged enzyme from Escherichia coli strain M15 by nickel affinity chromatography and gel filtration
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli M15 cells
gene asd, phylogenetic analysis
gene asd, subcloning in Escherichia coli strain JM109, DNA sequence determination and analysis, optimization of functional overexpression in Escherichia coli strain M15 as His-tagged protein
heterologous expression in Escherichia coli
expression of His-tagged enzyme in Escherichia coli strain M15
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
medicine
enzyme is a validated drug target
pharmacology
inhibitor design from enzyme three-dimensional structure
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Shafiani, S.; Sharma, P.; Vohra, R.M.; Tewari, R.
Cloning and characterization of aspartate-beta-semialdehyde dehydrogenase from Mycobacterium tuberculosis H37 Rv
J. Appl. Microbiol.
98
832-838
2005
Mycobacterium tuberculosis (P9WNX5), Mycobacterium tuberculosis, Mycobacterium tuberculosis H37Rv (P9WNX5), Mycobacterium tuberculosis H37Rv
Manually annotated by BRENDA team
Vyas, R.; Kumar, V.; Panjikar, S.; Karthikeyan, S.; Kishan, K.V.; Tewari, R.; Weiss, M.S.
Purification, crystallization and preliminary X-ray diffraction analysis of aspartate semialdehyde dehydrogenase (Rv3708c) from Mycobacterium tuberculosis
Acta Crystallogr. Sect. F
64
167-170
2008
Mycobacterium tuberculosis, Mycobacterium tuberculosis (P9WNX5), Mycobacterium tuberculosis H37Rv (P9WNX5)
Manually annotated by BRENDA team
Singh, A.; Kushwaha, H.R.; Sharma, P.
Molecular modelling and comparative structural account of aspartyl beta-semialdehyde dehydrogenase of Mycobacterium tuberculosis (H37Rv)
J. Mol. Model.
14
249-263
2008
Mycobacterium tuberculosis (P9WNX5), Mycobacterium tuberculosis, Mycobacterium tuberculosis H37Rv (P9WNX5)
Manually annotated by BRENDA team
Vyas, R.; Tewari, R.; Weiss, M.S.; Karthikeyan, S.
Structures of ternary complexes of aspartate-semialdehyde dehydrogenase (Rv3708c) from Mycobacterium tuberculosis H37Rv
Acta Crystallogr. Sect. D
68
671-679
2012
Mycobacterium tuberculosis (P9WNX5), Mycobacterium tuberculosis H37Rv (P9WNX5), Mycobacterium tuberculosis H37Rv
Manually annotated by BRENDA team
Meng, J.; Yang, Y.; Xiao, C.; Guan, Y.; Hao, X.; Deng, Q.; Lu, Z.
Identification and validation of aspartic acid semialdehyde dehydrogenase as a new anti-Mycobacterium tuberculosis target
Int. J. Mol. Sci.
16
23572-23586
2015
Mycobacterium tuberculosis, Mycobacterium tuberculosis H37Rv
Manually annotated by BRENDA team
Khan, S.; Somvanshi, P.; Bhardwaj, T.; Mandal, R.K.; Dar, S.A.; Wahid, M.; Jawed, A.; Lohani, M.; Khan, M.; Areeshi, M.Y.; Haque, S.
Aspartate-beta-semialdeyhyde dehydrogenase as a potential therapeutic target of Mycobacterium tuberculosis H37Rv Evidence from in silico elementary mode analysis of biological network model
J. Cell. Biochem.
119
2832-2842
2018
Mycobacterium tuberculosis (P9WNX5), Mycobacterium tuberculosis ATCC 25618 (P9WNX5), Mycobacterium tuberculosis H37Rv (P9WNX5)
Manually annotated by BRENDA team