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Literature summary for 3.1.7.2 extracted from

  • Avarbock, A.; Avarbock, D.; Teh, J.S.; Buckstein, M.; Wang, Z.m.; Rubin, H.
    Functional Regulation of the Opposing (p)ppGpp Synthetase/Hydrolase Activities of RelMtb from Mycobacterium tuberculosis (2005), Biochemistry, 44, 9913-9923.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
expression of fragment proteins in Escherichia coli BL21(DE3) Mycobacterium tuberculosis

Engineering

Protein Variants Comment Organism
D81A loss of hydrolytic activity with retention of synthesis Mycobacterium tuberculosis
G241E loss of synthetic activity and retention of hydrolysis Mycobacterium tuberculosis
H344Y loss of synthetic activity and retention of hydrolysis Mycobacterium tuberculosis
H80A loss of hydrolytic activity with retention of synthesis Mycobacterium tuberculosis
DELTA395-738 frament contains both synthesis and hydrolysis activities Mycobacterium tuberculosis
DElTA1-86/DELTA395-738 contains only (p)ppGpp synthesis activity, no hydrolysis activity Mycobacterium tuberculosis
DELTA182-738 fragment contains only (p)ppGpp hydrolysis activity, no synthesis activity Mycobacterium tuberculosis

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
additional information
-
Mycobacterium tuberculosis

Organism

Organism UniProt Comment Textmining
Mycobacterium tuberculosis
-
-
-

Purification (Commentary)

Purification (Comment) Organism
fragments of the relMtb protein Mycobacterium tuberculosis

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
pppGpp + H2O
-
Mycobacterium tuberculosis pppG + diphosphate
-
r

Synonyms

Synonyms Comment Organism
(p)ppGpp synthetase/hydrolase
-
Mycobacterium tuberculosis