5.6.1.1: microtubule-severing ATPase
This is an abbreviated version!
For detailed information about microtubule-severing ATPase, go to the full flat file.
Word Map on EC 5.6.1.1
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5.6.1.1
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spastic
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hereditary
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kinesins
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paraplegia
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mitotic
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cortical
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cytoskeleton
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disassembly
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centrosome
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gelsolin
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corticospinal
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atpases
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cytokine
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paraparesis
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atlastin
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microtubule-based
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actin-binding
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microtubule-binding
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escrt-iii
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antimitotic
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axonopathy
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minus-ends
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gamma-tubulin
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kinesin-related
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plus-ends
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mt-associated
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microtubule-dependent
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phragmoplasts
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midbody
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medicine
- 5.6.1.1
- spastic
- hereditary
- kinesins
- paraplegia
-
mitotic
- cortical
- cytoskeleton
-
disassembly
- centrosome
- gelsolin
-
corticospinal
- atpases
- cytokine
- paraparesis
-
atlastin
-
microtubule-based
-
actin-binding
-
microtubule-binding
-
escrt-iii
-
antimitotic
-
axonopathy
-
minus-ends
- gamma-tubulin
-
kinesin-related
-
plus-ends
-
mt-associated
-
microtubule-dependent
-
phragmoplasts
- midbody
- medicine
Reaction
n ATP
+
n H2O
+
Synonyms
adseverin, Arabidopsis thaliana katanin small subunit, AtKSS, D-spastin, DGL1, Dm-Kat60, Drosophila katanin Dm-Kat60, EC 3.6.4.3, kananin, Kat60, katanin, KATANIN 1, katanin p60, katanin p60 ATPase-containing subunit A1, katanin p60 microtubule-severing protein, KATNAL1, kinesin spindle protein, kp60-NTD, KSP, mei-1, MEI-1/MEI-2 complex, MEI-1/MEI-2 katanin complex, microtuble severing AAA ATPase spastin, microtuble-severing AAA ATPase, microtuble-severing ATPase spastin, microtubule severing protein, microtubule-severing AAA ATPase, microtubule-severing ATPase, microtubule-severing complex katanin, microtubule-severing complex MEI-1/MEI-2 katanin, microtubule-severing protein, microtubule-stimulated ATPase, MT-severing AAA ATPase, P60, p60 KAT1p, p60 katanin, P60-kananin, P60-katanin, p81-p60, Pf15, plant microtubule-severing protein, rice KTN1, scinderin, SPAS-1, spastin, spastin AAA domain, SPG4, Sug1p, vertebrate katanin
ECTree
5.6.1.1 microtubule-severing ATPaseAdvanced search results
results (
results (Engineering
Engineering on EC 5.6.1.1 - microtubule-severing ATPase
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PROTEIN VARIANTS 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
K437P/K441P
predicted not to form the C-terminal alpha-helix, microtuble network remains in mutant protein expressing HEK293 cells
1-279STOP
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deletion mutant, no severing of microtubules, no binding of microtubules
1-328STOP
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deletion mutant, no severing of microtubules, but binding of microtubules
DELTAMTBD
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deletion mutant lacking aa 1-227 and 270-328, neither binds nor severs microtubules
E356A
the basal ATPase activity is severely compromised to undetectable levels
E442Q
fragment 227-279
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fragment consisting of aa 227-279, no severing of microtubules, no binding of microtubules
fragment 227-328
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fragment consisting of aa 227-328, no severing of microtubules, but binding of microtubules
K388R
P45Q
leading to an early onset severe form of hereditary spastic paraplegia when present in heterozygosity with a mutant allele
R499C
R562Q
the basal ATPase activity is severely compromised to undetectable levels
S44L
leading to an early onset severe form of hereditary spastic paraplegia when present in heterozygosity with a mutant allele
K255A
A323V
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mutant dgl1-1, exhibits different response to gibberellin and/or brassinosteroid
D483N
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mutant dgl1-2, exhibits different response to gibberellin and/or brassinosteroid
DELTA241-408
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mutant dgl1-3, exhibits different response to gibberellin and/or brassinosteroid
additional information
E442Q
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mutant harboring a canonical Walker B motif point mutation, predicted to bind but not hydrolyze ATP
E442Q
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residue of Walker B motif, hydrolysis deficient mutant, amino acid residues 228-616
E442Q
neutralization of the positive charges in the microtubule-binding domain (MTBD) of spastin, resulting in the spastin-allA mutant, dramatically decreases the ATPase activity at low concentration, although the ATP-hydrolyzing potential is not affected. The ATP-hydrolyzing activity of spastin-allA is stimulated to varying levels by the ATPase-deficient E442Q mutant, depending on whether the microtubule-binding domain is intact
K255A
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mutant, dominant inhibitor of mouse p60, fused with RFP driven by CMV promoter
additional information
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homozygotic gene disruption mutants, meiotic spindles move to the cortex, but association with cortex is unstable
additional information
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mei-1(null): mutant lacking katanin activity, mei-1(gf): gain-of-function mutant
additional information
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mutational analysis reveals that the conserved exposed, basic amino acid residues in the pore region of stastin as well as the aromatic residue are important for the recognition and severing of microtubules. The conformational change of W251 is detected upon ATP binding by measuring the fluorescence emission spectra of tryptophan. Given that K257 is located close to the corresponding aromatic residue W251, it seems possible that K257 is also involved in a mechanochemical process from conformational change of W251 in microtubule severing
additional information
C-terminal deletion mutants: 1-432, 1-435, 1-447, C-terminal alpha-helix is essential for microtuble severing
additional information
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C-terminal deletion mutants: 1-432, 1-435, 1-447, C-terminal alpha-helix is essential for microtuble severing
additional information
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deltaTM D-spastin-GFP: construct lacking the transmembrane-containing N-terminus, diffusely distributed in the cytoplasm, fully active for disassembling cytoplasmatic microtubules. TM+MIT: construct lacking the AAA domain, do not affect the microtubule cytoskeleton. MIT: MIT domain alone, diffusely distributed and do not disassemble microtubules. AAA: AAA domain alone, diffusely distributed and do not disassemble microtubules.
additional information
expression of a dominant-negative enzyme construct inhibits microtubule severing and is deleterious to axonal growth. Overexpression of wild-type enzyme results in excess microtubule severing and is also deleterious to axonal growth in some of the neurons
