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Literature summary for 7.4.2.5 extracted from

  • Hou, J.M.; DLima, N.G.; Rigel, N.W.; Gibbons, H.S.; McCann, J.R.; Braunstein, M.; Teschke, C.M.
    ATPase activity of Mycobacterium tuberculosis SecA1 and SecA2 proteins and its importance to SecA2 function in macrophages (2008), J. Bacteriol., 190, 4880-4887.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

Cloned (Comment) Organism
-
Escherichia coli
into the pET29a vector for expression in Escherichia coli BL21DE3 cells Mycobacterium tuberculosis
into the pET41b vector for expression in Escherichia coli BL21DE3 cells Mycobacterium tuberculosis

Protein Variants

Protein Variants Comment Organism
K108R mutant, defective in ATP binding and protein translocation in vitro, as well as biologically inactive in vivo Escherichia coli
K115A mutant, substitution of the conserved lysine in the Walker A motif eliminates ATP binding and affects the biological activity Mycobacterium tuberculosis
K115R mutant, substitution of the conserved lysine in the Walker A motif eliminates ATP binding and affects the biological activity Mycobacterium tuberculosis

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
additional information ATP hydrolysis rate 10.5 nmol phosphate/min/nmol SecA1 Mycobacterium tuberculosis
additional information
-
additional information ATP hydrolysis rate SecA wild-type 6.1 nmol phosphate/min/nmol enzyme Escherichia coli
additional information
-
additional information ATP hydrolysis rate SecA2 wild-type 19.7, K115R mutant 25.0, K115A mutant 13.5 nmol Pi/min/nmol enzyme Mycobacterium tuberculosis

Localization

Localization Comment Organism GeneOntology No. Textmining
cytoplasm
-
Mycobacterium tuberculosis 5737
-
cytoplasm
-
Escherichia coli 5737
-
cytoplasmic membrane
-
Mycobacterium tuberculosis
-
-
cytoplasmic membrane
-
Escherichia coli
-
-

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
85400
-
monomer, predicted molecular mass, determined by SDS-PAGE Mycobacterium tuberculosis
95000
-
determined by SDS-PAGE Escherichia coli
101000
-
monomer, predicted molecular mass Escherichia coli
106000
-
monomer, predicted molecular mass, determined by SDS-PAGE Mycobacterium tuberculosis

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
ATP + H2O Mycobacterium tuberculosis
-
ADP + phosphate
-
ir
ATP + H2O Escherichia coli
-
ADP + phosphate
-
ir
ATP + H2O Mycobacterium tuberculosis H37Rv
-
ADP + phosphate
-
ir

Organism

Organism UniProt Comment Textmining
Escherichia coli P10408
-
-
Mycobacterium tuberculosis P9WGP3
-
-
Mycobacterium tuberculosis P9WGP5
-
-
Mycobacterium tuberculosis H37Rv P9WGP3
-
-
Mycobacterium tuberculosis H37Rv P9WGP5
-
-

Purification (Commentary)

Purification (Comment) Organism
-
Escherichia coli
using a Blue-Sepharose CL-6B column Mycobacterium tuberculosis

Source Tissue

Source Tissue Comment Organism Textmining

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + H2O
-
Mycobacterium tuberculosis ADP + phosphate
-
ir
ATP + H2O
-
Escherichia coli ADP + phosphate
-
ir
ATP + H2O
-
Mycobacterium tuberculosis H37Rv ADP + phosphate
-
ir

Synonyms

Synonyms Comment Organism
SecA
-
Escherichia coli
SecA ATPase
-
Escherichia coli
SecA1
-
Mycobacterium tuberculosis
SecA1 ATPase
-
Mycobacterium tuberculosis
SecA2
-
Mycobacterium tuberculosis
SecA2 ATPase
-
Mycobacterium tuberculosis

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
25
-
ATPase activity assay Mycobacterium tuberculosis

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7
-
ATPase activity assay Mycobacterium tuberculosis