3.4.21.64: peptidase K
This is an abbreviated version!
For detailed information about peptidase K, go to the full flat file.
Word Map on EC 3.4.21.64
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3.4.21.64
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3.4.21.4
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chymotrypsin
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subtilisins
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alpha-chymotrypsin
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carlsberg
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3.1.1.3
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synthesis
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degradation
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beta-trypsin
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diagnostics
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analysis
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pharmacology
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molecular biology
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medicine
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detergent
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3.4.17.1
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biotechnology
- 3.4.21.64
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3.4.21.4
- chymotrypsin
- subtilisins
- alpha-chymotrypsin
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carlsberg
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3.1.1.3
- synthesis
- degradation
- beta-trypsin
- diagnostics
- analysis
- pharmacology
- molecular biology
- medicine
- detergent
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3.4.17.1
- biotechnology
Reaction
Hydrolysis of keratin, and of other proteins with subtilisin-like specificity. Hydrolyses peptide amides =
Synonyms
EC 3.4.21.14, EC 3.4.21.4, EC 3.4.4.16, endopeptidase K, mesophilic proteinase K, PROK, Proteinase K, Proteinase, Tritirachium album serine, Tritirachium album proteinase K, Tritirachium alkaline proteinase
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General Information on EC 3.4.21.64 - peptidase K
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GENERAL INFORMATION 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
evolution
metabolism
physiological function
additional information
evolution
proteinase K belongs to the class of subtilisin-like serine protease with the typical triad of Asp39-His69-Ser224. The protein is folded into alpha- and beta-rich regions without any clear domains
metabolism
the central event in prion infection is the conformational conversion of host-encoded cellular prion protein into the pathogenic isoform. For the in vitro replication of pathogenic prion protein by protein-misfolding cyclic amplification, cofactors are required that are not produced by lower organism, e.g. insects, but by mammalia, e.g. C57BL/6J mice. Brain-derived factors are also necessary for the in vitro replication of glycosylphosphatidylinositol-anchored baculovirus-derived recombinant prion protein. Cofactor activity of insect cell lysates becomes functional after proteinase K digestion and heat treatment, following protease digestion and heat treatment, insect cell lysates had the functional cofactor activity required for Bac-prion protein replication by protein-misfolding cyclic amplification. Not only RNA, but also DNA, are the key components of protein-misfolding cyclic amplification, although other cellular factors were necessary for the expression of the cofactor activity of nucleic acids in insect cells
metabolism
SPE-8 class proteins, such as Pron and ProK, act in the hermaphrodite- and male-dependent spermiogenesis pathways. Some spermatid proteins presumably working downstream of spermiogenesis pathways, including MAP kinases, are preferentially involved in the SPE-8 class-dependent pathway. Construction of a model in which Caenorhabditis elegans male and hermaphrodite spermiogenesis each has its own distinct, parallel pathway. proteinase K (ProK), a bacterial serine protease, can activate the SPE-8 class-independent pathway, SPE-8 class-dependent and class-independent pathways, overview. The spe-8 class genes are involved in both hermaphrodite- and male-dependent spermiogenesis and MAPKs are preferentially involved in the Pron- and Zn2+-activated SPE-8 class-dependent pathways
physiological function
proteinase K eliminate DNA from injured or dead bacteria but not from living bacteria in microbial reference systems and natural drinking water biofilms
physiological function
proteinase K (ProK) is an activator for the male-dependent spermiogenesis pathway in Caenorhabditis elegans. Caenorhabditis elegans spermiogenesis involves spermatid activation into spermatozoa. Activation occurs through either SPE-8 class-dependent or class-independent pathways. The microbe-derived serine protease ProK can also induce spermiogenesis in male-derived spermatids from N2 and spe-8 class mutants, i.e. spe-8(hc40), spe-12(hc76), spe-19(eb52) and spe-27(it110)
additional information
nonspecific protease proteinase K can be used as an alternative to trypsin for cross-linking studies, digestion by proteinase K results in a family of related cross-linked peptides, all of which contained the same cross-linking sites, thus providing additional verification of the cross-linking results. Using proteinase K, the affinity-purifiable CID-cleavable and isotopically coded cross-linker cyanurbiotindipropionylsuccinimide and MALDI-MS cross-links are found for all of the possible cross-linking sites of native and oligomeric forms of prion protein substrates, overview. After digestion with proteinase K, the mass distribution of the crosslinked peptides is very suitable for MALDI-MS analysis, detailed overview of cross-links in prion proteins
additional information
proteinase K-resistant Bac-prion protein is generated by protein-misfolding cyclic amplification using insect cells expressing the protein and prionprotein null mouse brain homogenate
additional information
dynamics of serine protease proteinase K, and effect of the solvent temperatures, proteinase K structure-function analysis, simulations, detailed overview
additional information
the catalytic triad and oxyanion hole of proteinase K are formed by Asp39, His69 and Ser224, and Asn161, respectively. Furthermore, two segments Asn99-Tyr104 and Ser132-Gly136 form substrate recognition site of proteinase K. Spermine quenches the intensity of proteinase K with static mechanism. Molecular docking using structure PDB ID 2ID8
additional information
carboxylic acids and compounds, e.g. chrysanthemin, quercetin, and valerenic acid, in Sambucus nigra plant extract can create stable Cu-carboxylic acid complexes. CuO nanoparticles, synthesized using Sambucus nigra (elderberry) fruit extract, bind proteinase K, and induce structural changes in enzyme accompanied by a decrease in Michaelis-Menten constant at 25°C. The enzyme affinity for the substrate is increased. Depending on the temperature, CuO nanoparticles show a dual effect on the thermodynamic stability and binding affinity of enzyme. The nanoparticles increase the stability of the native state of enzyme at room temperature. On the other hand, the nanoparticles stabilize the unfolded state of enzyme at 37-50°C. An overall favorable Gibbs energy change is observed for the binding process at 25-50°C. The enzyme-nanoparticle binding is enthalpically driven at room temperature. Hydrogen bonding plays a key role in the interaction of enzyme with nanoparticles at 25-37°C. At higher temperatures, the protein-ligand binding is entropically driven. Thus hydrophobic association plays a major role in the proteinase K-CuO binding at 37-50°C. Thermodynamics, overview
