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Search results 401 to 463 out of 463 for Pim1

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Type Details Score
Protein
Organism: Mus musculus/domesticus
Length: 115  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 389  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 651  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 172  
Fragment?: true
Protein
Organism: Mus musculus/domesticus
Length: 882  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 79  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 461  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 680  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 69  
Fragment?: true
Protein
Organism: Mus musculus/domesticus
Length: 557  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 157  
Fragment?: true
Protein
Organism: Mus musculus/domesticus
Length: 116  
Fragment?: true
Protein
Organism: Mus musculus/domesticus
Length: 168  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 421  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 972  
Fragment?: false
Publication
First Author: Tojo N
Year: 1993
Journal: J Bacteriol
Title: The lonD gene is homologous to the lon gene encoding an ATP-dependent protease and is essential for the development of Myxococcus xanthus.
Volume: 175
Issue: 14
Pages: 4545-9
Protein Domain
Type: Active_site
Description: Proteolytic enzymes that exploit serine in their catalytic activity are ubiquitous, being found in viruses, bacteria and eukaryotes []. They include a wide range of peptidase activity, including exopeptidase, endopeptidase, oligopeptidase and omega-peptidase activity. Many families of serine protease have been identified, these being grouped into clans on the basis of structural similarity and other functional evidence []. Structures are known for members of the clans and the structures indicate that some appear to be totally unrelated, suggesting different evolutionary origins for the serine peptidases [].Not withstanding their different evolutionary origins, there are similarities in the reaction mechanisms of several peptidases. Chymotrypsin, subtilisin and carboxypeptidase C have a catalytic triad of serine, aspartate and histidine in common: serine acts as a nucleophile, aspartate as an electrophile, and histidine as a base []. The geometric orientations of the catalytic residues are similar between families, despite different protein folds []. The linear arrangements of the catalytic residues commonly reflect clan relationships. For example the catalytic triad in the chymotrypsin clan (PA) is ordered HDS, but is ordered DHS in the subtilisin clan (SB) and SDH in the carboxypeptidase clan (SC) [, ].This signature defines the active site of the serine peptidases belonging to the MEROPS peptidase family S16 (lon protease family, clan SF). These proteases which are dependent on the hydrolysis of ATP for their activity and have a serine in their active site, they include:Bacterial ATP-dependent proteases [, ]. The prototype of those bacterial enzymes is the Escherichia coli La protease () (gene lon). La is capable of hydrolysing large proteins; it degrades short-lived regulatory (such as rcsA and sulA) and abnormal proteins. It is a cytoplasmic protein of 87kDa that associates as an homotetramer. Its proteolytic activity is stimulated by single-stranded DNA.Eukaryotic mitochondrial matrix proteases [, ]. The prototype of these enzymes is the yeast PIM1 protease. It is a mitochondrial matrix protein of 120kDa that associated as an homohexamer. It catalyses the initial step of mitochondrial protein degradation.Haemophilus influenzae lon-B (HI1324), a protein which does not contain the ATP-binding domain, but possess a slightly divergent form of the catalytic domain.
Protein
Organism: Mus musculus/domesticus
Length: 445  
Fragment?: false
Publication
First Author: Thomas CD
Year: 1993
Journal: Gene
Title: Controlled high-level expression of the lon gene of Escherichia coli allows overproduction of Lon protease.
Volume: 136
Issue: 1-2
Pages: 237-42
Protein
Organism: Mus musculus/domesticus
Length: 589  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 531  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 551  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 949  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 852  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 1003  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 1057  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 913  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 517  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 938  
Fragment?: true
Protein
Organism: Mus musculus/domesticus
Length: 391  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 953  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 1050  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 913  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 531  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 1050  
Fragment?: false
Publication
First Author: Roudiak SG
Year: 1998
Journal: Biochemistry
Title: The lon protease from Mycobacterium smegmatis: molecular cloning, sequence analysis, functional expression, and enzymatic characterization.
Volume: 37
Issue: 1
Pages: 377-86
Publication
First Author: Chin DT
Year: 1988
Journal: J Biol Chem
Title: Sequence of the lon gene in Escherichia coli. A heat-shock gene which encodes the ATP-dependent protease La.
Volume: 263
Issue: 24
Pages: 11718-28
Publication
First Author: Fischer H
Year: 1993
Journal: J Biol Chem
Title: ATP hydrolysis is not stoichiometrically linked with proteolysis in the ATP-dependent protease La from Escherichia coli.
Volume: 268
Issue: 30
Pages: 22502-7
Publication
First Author: Robertson GT
Year: 2000
Journal: Mol Microbiol
Title: The Brucella abortus Lon functions as a generalized stress response protease and is required for wild-type virulence in BALB/c mice.
Volume: 35
Issue: 3
Pages: 577-88
Publication
First Author: Lee I
Year: 2006
Journal: Mol Biosyst
Title: Recent developments in the mechanistic enzymology of the ATP-dependent Lon protease from Escherichia coli: highlights from kinetic studies.
Volume: 2
Issue: 10
Pages: 477-83
Protein
Organism: Mus musculus/domesticus
Length: 414  
Fragment?: true
Protein
Organism: Mus musculus/domesticus
Length: 1352  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 446  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 160  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 495  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 309  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 762  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 753  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 837  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 754  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 518  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 984  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 1005  
Fragment?: true
Protein
Organism: Mus musculus/domesticus
Length: 1651  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 698  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 432  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 4859  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 4836  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 4749  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 4636  
Fragment?: true
Protein
Organism: Mus musculus/domesticus
Length: 4746  
Fragment?: false
Publication  
First Author: Rawlings ND
Year: 1994
Journal: Methods Enzymol
Title: Families of serine peptidases.
Volume: 244
Pages: 19-61
Publication  
First Author: Rawlings ND
Year: 1993
Journal: Biochem J
Title: Evolutionary families of peptidases.
Volume: 290 ( Pt 1)
Pages: 205-18