3.4.17.12: carboxypeptidase M
This is an abbreviated version!
For detailed information about carboxypeptidase M, go to the full flat file.
Word Map on EC 3.4.17.12
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3.4.17.12
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pain
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women
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lymphocyte
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contralateral
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children
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postoperative
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prophylactic
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myelinolysis
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mastectomy
-
pontine
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knee
-
cyclophosphamide
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unilateral
-
wave
-
rehabilitation
-
hyponatremia
-
decision
-
summation
-
session
-
flexion
-
accelerometer
-
myoelectrical
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chlorpheniramine
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preoperative
-
arthroplasty
-
noxious
-
phytohemagglutinin
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3h-thymidine
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maleate
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pressor
-
pain-free
-
decision-making
-
analgesia
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psychophysical
-
actigraph
-
pokeweed
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moderate-to-vigorous
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3h-tdr
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disomy
-
myotomy
-
cuff
-
physiotherapy
-
arthroscopic
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gastroparesis
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suprathreshold
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dysrhythmias
-
breast-conserving
-
medicine
-
trapezius
-
manometry
-
resting-state
-
diagnostics
- 3.4.17.12
- pain
- women
- lymphocyte
-
contralateral
- children
-
postoperative
-
prophylactic
- myelinolysis
-
mastectomy
- pontine
- knee
- cyclophosphamide
-
unilateral
-
wave
-
rehabilitation
- hyponatremia
-
decision
-
summation
-
session
-
flexion
-
accelerometer
-
myoelectrical
-
chlorpheniramine
-
preoperative
-
arthroplasty
-
noxious
- phytohemagglutinin
-
3h-thymidine
- maleate
-
pressor
-
pain-free
-
decision-making
-
analgesia
-
psychophysical
-
actigraph
-
pokeweed
-
moderate-to-vigorous
-
3h-tdr
-
disomy
-
myotomy
-
cuff
-
physiotherapy
-
arthroscopic
-
gastroparesis
-
suprathreshold
- dysrhythmias
-
breast-conserving
- medicine
-
trapezius
-
manometry
-
resting-state
- diagnostics
Reaction
cleavage of C-terminal arginine or lysine residues from polypeptides =
Synonyms
carboxypeptidase M, carboxypeptidase-M, CPM, M14006 (Merops-ID), More
ECTree
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Engineering
Engineering on EC 3.4.17.12 - carboxypeptidase M
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E260A
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mutation reduces the ratio of turnover-numver to Km-value by 104fold and further decreases stability.Addition of 0.5 M NaCl to the assay buffer does not significantly alter the activities of the wild-type enzyme with 0.2 mM dansyl-Ala-Arg or the E260Q mutant enzyme but does substantially increase the activity of the E260A mutant, 219%. The enhancement of E260A is not specific for NaCl, as similar increases are detected with other salts such as NaNO3, 249%, KNO3, 256%, KCl, 256%, or Na2SO4, 297%
E260Q
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mutation has minimal effects on kinetic parameters, but decreased heat stability
E264Q
S406A
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very similar to the wild-type enzyme with regard to expression and release by phosphatidylinositol-specific phospholipase C
S406P
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the wild-type and S406A and S406T mutants are expressed on the plasma membrane in glycosylphosphatidylinositol-anchored form, the S406P mutant is not and is retained in a perinuclear location
S406T
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very similar to the wild-type enzyme with regard to expression and release by phosphatidylinositol-specific phospholipase C
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mutation results in a 10000fold decrease in activity, but the enzyme still binds to p-aminobenzoylarginine-Sepharose and is resistant to trypsin treatment, indicating that the protein is folded properly