EC Number   |
Recommended Name |
Application |
|---|
   3.4.21.9 | enteropeptidase |
molecular biology |
the high specificity of the target site makes enterokinase an ideal tool for cleaving fusion proteins at defined cleavage sites |
| 3.4.21.61 | Kexin |
molecular biology |
role of Kex2 during cell fusion. Kex2 may promote cell fusion by proteolytically processing substrates that act in parallel to Prm1 as an alternative fusion machine, as cell wall components, or both |
| 3.4.21.64 | peptidase K |
molecular biology |
proteinase K from Tritirachium album, which is one of the most widely used proteases in molecular biological studies. The synthesized linear oligo-phenylalanine shows a unique self-assembly in aqueous solutions |
| 3.4.21.86 | Limulus clotting enzyme |
molecular biology |
laser scattering photometry can be used to measure the formation of small particles of clotted enzyme, the timing is related to endotoxin concentration, this method can be used for quick and sensitive endotoxin assay |
| 3.4.21.91 | Flavivirin |
molecular biology |
it is demonstrated that the WNV NS2B/NS3pro-hel is an active endoproteolytic enzyme at the ER membrane and the in-cell selectivity profiling of the membrane-anchored flaviviral protease is reported |
| 3.4.21.94 | proprotein convertase 2 |
molecular biology |
the regulation of the prohormone processing system by morphine may lead to alterations in the levels of multiple bioactive hormones and may be a compensatory mechanism whereby the organism tries to restore its homeostatic hormonal milieu. The down-regulation of PC1/3, PC2 and P-CREB by short-term morphine and up-regulation by long-term morphine treatment may be a signal mediating the switch from drug use to drug abuse |
| 3.4.21.98 | hepacivirin |
molecular biology |
in order to develop an efficient screening method to identify viral proteins and their ability to block Jak-Stat signaling, the 2FTGH (human fibrosarcoma cells) cell assay system is used in combination with transient transfection of hepatitis C virus proteins: Using 1000 U/ml interferon and 30 mM 6-thioguanine to treat 2FTGH cells, it is established that transient protein expression in this cell system yields 39% and 0% cell survival for the positive (HPV E7) and negative controls (GFP expression) respectively. Transient expression of HCV Core-p7 results in 22% cell survival, consistent with previous reports, while expression of the HCV serine protease NS3/4a results in 54% cell survival. Furthermore, it is shown that NS3/4a inhibits phosphorylation of Stat-1 at the serine residue |
| 3.4.21.104 | mannan-binding lectin-associated serine protease-2 |
molecular biology |
near monodisperse endotoxin-free polyethylene glycol, at concentrations relevant to therapeutic effects, trigger complement activation in human sera. Depending on polyethylene glycol concentration and average molecular weight, complement activation proceeds either exclusively through MASP-2 activation, and a likely role for the lectin pathway, or through both MASP-2-mediated C4 cleavage and accelerated alternative pathway turnover |
| 3.4.21.105 | rhomboid protease |
molecular biology |
TM5 helix and L1 loop are dynamically coupled so that changes in the dynamics of one are relayed to the other |
| 3.4.21.107 | peptidase Do |
molecular biology |
htrA gene in Porphyromonas gingivalis does not relate to stress conditions such as high temperature and pH, but rather to H2O2 stress. The htrA gene is important for virulence and survival in in vivo animal models |
| 3.4.21.107 | peptidase Do |
molecular biology |
instead of using an Lactococcus lactis htrA mutant, the reduction of the HtrA level in wild-type recombinant cultures of Lactococcus lactis by acid tolerace response (ATR) suppression may serve as a better strategy for the production of secreted recombinant proteins |
| 3.4.21.117 | stratum corneum chymotryptic enzyme |
molecular biology |
an activity assay for human kallikrein 7 is developed using a blue-fluorescent acridone dye, featuring a remarkably long lifetime that can be quenched by either of the 2 natural amino acids, tyrosine and tryptophan. Incorporating this probe and 1 of the quenching amino acids on either side of the scissile bond of the substrate peptide makes it possible to monitor the enzymatic activity by quantifying the increase in the fluorescence lifetime signal. A systematic investigation of substrate structures leads to a homogenous, microplate-based, compound profiling assay that yields inhibitory constants down into the single-digit nanomolar range |
| 3.4.21.117 | stratum corneum chymotryptic enzyme |
molecular biology |
kallikrein 7 and antileukoprotease are down-regulated in prostate cancers |
| 3.4.21.117 | stratum corneum chymotryptic enzyme |
molecular biology |
kallikrein 7 may play a critical role in the invasion of cancer cells in which it is aberrantly expressed by degrading important cell adhesive molecules like desmogleins and E-cadherin |
| 3.4.21.118 | kallikrein 8 |
molecular biology |
miRNAs play a role in the regulation of KLK expression: using a bioinformatics approach 96 strong KLK/miRNA interactions are identified. KLK10 is the most frequently targeted kallikrein, followed by KLK5 and KLK13. KLK1, KLK3, KLK8 and KLK12 do not have strongly predicted miRNA/KLK interactions |
| 3.4.21.122 | transmembrane protease serine 2 |
molecular biology |
establishement of MDCK cell lines stably expressing TMPRSS2. The cell line stably expresses TMPRSS2 after 20 serial passages |
| 3.4.22.1 | cathepsin B |
molecular biology |
N,N'-diBoc-dityrosine-Gly-(isoniazid)2 is a sensitive and selective assay of cathepsin B activity |
| 3.4.22.14 | actinidain |
molecular biology |
actinidin compared with type II or IV collagenase isolates intact human umbilical vein endothelial cells, hepatocytes, and thymic epithelial cells with viability more than 90% |
| 3.4.22.28 | picornain 3C |
molecular biology |
a protein-tagging system for purification of EGFP from Escherichia coli using a single-step glutathione column purification and release of EGFP from the column using a variant of Human Rhinovirus 14 3C is described. A biotinylated variant of Human Rhinovirus 14 3C protease (bHR3Cp) is constructed, which includes a factor Xa or thrombin cleavage site between the protease gene and the biotinylation signal. This system readily allows attachment of the protease to a variety of surfaces and subsequent release using either thrombin or factor Xa proteases |
| 3.4.22.28 | picornain 3C |
molecular biology |
human rhinovirus (HRV) 3C protease is widely used in recombinant protein production for various applications such as biochemical characterization and structural biology projects to separate recombinant fusion proteins from their affinity tags in order to prevent interference between these tags and the target proteins |
| 3.4.22.29 | picornain 2A |
molecular biology |
picornaviral 2A sequences can be used to express transgenes in oncolytic adenoviruses |
| 3.4.22.37 | gingipain R |
molecular biology |
enzyme is a convenient tool for protein chemistry due to its stability and activity under conditions of high detergent concentration used in protein solubilization and purification |
| 3.4.22.47 | gingipain K |
molecular biology |
a combination of both R- and K-gingipains is required for pigment production from oxyhemoglobin by Porphyromonas gingivalis since R-gingipain converts oxyhemoglobin into the methemoglobin form which is more susceptible to Kgp degradation for the eventual release of iron(III) protoporphyrin IX and production of the micro-oxo haem dimer |
| 3.4.22.47 | gingipain K |
molecular biology |
it is shown that the production of anionic polysaccharide at the surface of Porphyromonas gingivalis rather than Arg- and Lys-gingipain synthesis is the principal mechanism of serum resistance in Porphyromonas gingivalis |
| 3.4.22.49 | separase |
molecular biology |
data suggest that the co-ordinated expression of separase, securin and Rad21 is fundamental for the developing brain |
| 3.4.22.49 | separase |
molecular biology |
in Saccharomyces cerevisiae separase it is shown that separase is implicated in a second non-proteolytic pathway: separsae is essential for the activation of Cdc14 phosphatase and thus a broad programme of late mitotic events culminating in mitotic exit and cell division |
| 3.4.22.49 | separase |
molecular biology |
separase is identified as a key cell cycle component that is required for degranulation |
| 3.4.22.49 | separase |
molecular biology |
separse is not only required for chromosome segregation but also for meiotic exit |
| 3.4.22.49 | separase |
molecular biology |
the results indicate that inhibitory phosphorylation of separase plays a critical role in the maintenance of sister chromatid cohesion and genome stability in proliferating postmigratory primordial germ cells |
| 3.4.22.49 | separase |
molecular biology |
the results show that a fraction of arm cohesin is protected by Sgo1, which prevents cohesin from being removed by the prophase pathway, and that separase is partly activated in nocodazole-arrested cells and removes the arm cohesion protected by Sgo1 |
| 3.4.22.51 | cruzipain |
molecular biology |
in this study it is shown in murine macrophage cell line J774 as well as in murine bone marrow-derived macrophages, that cruzipain induces p38 phosphorylation with Trypanosoma cruzi infection triggering mainly JNK and ERK phosphorylation. Cruzipain also favors the survival in macrophages by changing the iNOS/arginase balance |
| 3.4.22.56 | caspase-3 |
molecular biology |
engineering of CHO cells for more robust cell lines includes reduction of apoptotic capase-3, overview |
| 3.4.22.59 | caspase-6 |
molecular biology |
heat sensitive expression of caspase-6 in the embryonic heart is of interest since cardiac malformations are an emergent problem in salmon aquaculture |
| 3.4.22.59 | caspase-6 |
molecular biology |
it is shown that caspase-6 is the major caspase responsible for the death of cells infected with Adeno-associated virus (AAV) infection |
| 3.4.22.59 | caspase-6 |
molecular biology |
it is shown that trifolin acetate-induced cell death in human leukemia cells is dependent on caspase-6 |
| 3.4.22.59 | caspase-6 |
molecular biology |
the results show that caspase-1 is an upstream positive regulator of caspase-6-mediated cell death in primary human neurons |
| 3.4.22.60 | caspase-7 |
molecular biology |
engineering of CHO cells for more robust cell lines includes reduction of apoptotic capase-7, overview |
| 3.4.22.68 | Ulp1 peptidase |
molecular biology |
modification of recombinant proteins by SUMOylation often dramatically increases solubility and stability during expression of the fusion proteins in bacteria relative to unfused proteins. After expressing a protein as a fusion to SUMO, it is often desirable to cleave the SUMO off of the fusion protein using a SUMO-specific protease such as Ulp1. To facilitate such processing, a dual expression vector is constructed encoding two fusion proteins: one consisting of SUMO fused to Ulp1 and a second consisting of SUMO fused to a His-tagged protein of interest. The SUMO-Ulp1 cleaves both itself and the other SUMO fusion protein in the bacterial cells prior to lysis, and the proteins retain solubility after cleavage, method evaluation, overview |
| 3.4.22.68 | Ulp1 peptidase |
molecular biology |
usage of the targeting and small ubiquitin-like modifier, SUMO, binding properties of Ulp1(3)(C580S) to purify Smt3-modified proteins from cell extracts |
| 3.4.22.70 | sortase A |
molecular biology |
a general strategy for the site-specific modification of cell surface proteins with synthetic molecules by using sortase, a transpeptidase from Staphylococcus aureus. The short peptide tag LPETGG is genetically introduced to the C terminus of the target protein, expressed on the cell surface. Subsequent addition of sortase and an N-terminal triglycine-containing probe results in the site-specific labeling of the tagged protein. C-terminal-specific labeling of osteoclast differentiation factor with a biotin- or fluorophore-containing short peptide on the living cell surface. The labeling reaction occurrs efficiently in serum-containing medium, as well as serum-free medium or PBS. The labeled products are detected after incubation for 5 min. In addition, site-specific proteinprotein conjugation is successfully demonstrated on a living cell surface by the Sortase-catalyzed reaction. This strategy provides a powerful tool for cell biology and cell surface engineering |
| 3.4.22.70 | sortase A |
molecular biology |
method for immobilizing ligand proteins onto Biacore sensor chips using the transpeptidase activity of Staphylococcus aureus sortase A. This method provides a robust and gentle approach for the site-directed, covalent coupling of proteins to biosensor chips. The high specificity of the sortase allows immobilization of proteins from less than pure protein samples allowing short cuts in protein purification protocols |
| 3.4.23.B4 | Feline immunodeficiency virus protease |
molecular biology |
the FIV-PR mutant is a mutational model system to study the molecular basis of substrate-inhibitor specificity for lentivirus proteases, especially HIV-1 protease |
| 3.4.23.5 | cathepsin D |
molecular biology |
insights on the amino acid region involved in the terminal processing of human cathepsin D and on the function of the processing beta-hairpin loop are provided |
| 3.4.23.21 | Rhizopuspepsin |
molecular biology |
rhizopuspepsin is a good model enzyme to investigate acid proteinases |
| 3.4.23.34 | cathepsin E |
molecular biology |
CatE is a potential cancer biomarker |
| 3.4.23.39 | plasmepsin II |
molecular biology |
plasmepsin 2 but not plasmepsin 4 is a pential tool for hydrogen/deuterium exchange coupled to mass spectroscopy (DXMS) studies |
| 3.4.23.47 | HIV-2 retropepsin |
molecular biology |
an experimental model system based on the expression of HIV-2 protease in yeast cells is established: HIV-2 protease activity kills the yeast cell, this process can be abolished by inhibiting the viral enzyme activity |
| 3.4.24.11 | neprilysin |
molecular biology |
the established assay is extremely sensitive to neprilysin, but insensitive, or much less sensitive, to other Abeta-degrading enzymes. As low as 0.1 nM of neprilysin can be detected |
| 3.4.24.12 | envelysin |
molecular biology |
Ets4 is one of the transcription factors that control HE expression |
| 3.4.24.16 | neurolysin |
molecular biology |
neurolysin can be used as a molecular tool for analysis of properties of cancer-producing matrix metalloproteinases MMP-2 and MMP-9, quantitative determination of cleavage activity of neurolysin toward MMPspecific fluorescence-quenching peptides, overview |
| 3.4.24.20 | peptidyl-Lys metalloendopeptidase |
molecular biology |
biological application for enzyme-based proteolytic 18O labeling method characterizing the proteome changes of cytokine/lipolysaccharide-treated versus untreated human retinal pigment epithelium cell line |
| 3.4.24.20 | peptidyl-Lys metalloendopeptidase |
molecular biology |
proteolytic 18O labeling method employing enzyme for use in comparative proteomics. Enzyme incorporates only a single 18O atom into the carboxyl terminus of each proteolytically generated peptide. Method provides accurate quantification results for isotopically labeled peptides |
| 3.4.24.20 | peptidyl-Lys metalloendopeptidase |
molecular biology |
a method for detecting protein termini on both the amino and the carboxyl side, regardless of terminal modifications, such as N-acetylation is established. This method requires LC-MS/MS combined with two endopeptidases (lysyl endopeptidase) Lys-C and peptidyl-Lys metalloendopeptidase (Lys-N) |
| 3.4.24.33 | peptidyl-Asp metalloendopeptidase |
molecular biology |
many eukaryotic proteins are blocked at the alpha-amino group of their N-terminal with various modifications, thereby making it difficult to determine their N-terminal sequence by protein sequencer, development of a method for selectively isolating the blocked N-terminal peptide from the peptide mixture generated by endoproteinase AspN digestion of N-blocked protein by removal of all peptides other than the N-terminal one (non-N-terminal peptides) through their carbonyl group introduced by a chemical transamination reaction |
| 3.4.24.66 | choriolysin L |
molecular biology |
putative embryonic seCL148 product is most closely related to medaka choriolysin L |
| 3.4.24.69 | bontoxilysin |
molecular biology |
botulinum neurotoxins BoNT/A-G are widely used as laboratory research tools |
| 3.4.24.79 | pappalysin-1 |
molecular biology |
heparin administration is associated with a significant increase in PAPP-A levels, presumably because of the detachment of PAPP-A from the vessel wall |
| 3.4.24.79 | pappalysin-1 |
molecular biology |
mice born with the deletion of the gene for PAPP-A, a model of reduced local IGF activity, live approximately 30% longer than their wild-type littermates. Food intake, and total energy expenditure and resting energy expenditure as measured by calorimetry are not different between PAPP-A knockout and wild-type mice. There is an increase in spontaneous physical activity in PAPP-A knockout mice. Both wild-type and PAPP-A knockout mice exhibit mild insulin resistance with age. Oral glucose tolerance and insulin sensitivity are not significantly different between the two groups of mice, although there appeared to be a decrease in the average size of the pancreatic islets in PAPP-A knockout mice. Thus, neither reduced rate of living nor altered glucose-insulin homeostasis can be considered key determinants of the enhanced longevity of PAPP-A knockout mice |
| 3.4.24.81 | ADAM10 endopeptidase |
molecular biology |
ADAM10 is regulator of vascular permeability and possesses a function VE-cadherin-dependent endothelial cell functions and leukocyte transendothelial migration |
| 3.4.24.81 | ADAM10 endopeptidase |
molecular biology |
Kuzbanian, the ADAM10 orthologue in Drosophila melanogaster plays an important role in axon guidance by building a complex with ephrinA2, which is cleaved off from the membrane in a moment of EphA3 receptor binding |
| 3.4.24.81 | ADAM10 endopeptidase |
molecular biology |
tetraspanins regulate the activity of ADAM10 toward several substrates. It is illustrated how membrane compartmentalization by tetraspanins can control the function of cell surface proteins such as ectoproteases |
| 3.4.24.81 | ADAM10 endopeptidase |
molecular biology |
there is only a moderate alteration of gene expression in ADAM10 overexpressing mice. Genes coding for pro-inflammatory or pro-apoptotic proteins are not overrepresented among differentially regulated genes. Even a decrease of inflammation markers is observed. This further supports the strategy to treat alzheimers disease by increasing the beta-secretase activity |
| 3.4.24.83 | anthrax lethal factor endopeptidase |
molecular biology |
anthrax lethal toxin treatment of neutrophils disrupts signaling to downstream MAPK targets in response to TLR stimulation. Following anthrax lethal toxin treatment, ERK family and p38 phosphorylation are nearly completely blocked, but signaling to JNK family members persists in vitro and ex vivo. In contrast to previous reports involving human neutrophils, anthrax lethal toxin treatment of murine neutrophils increases their production of superoxide in response to PMA or TLR stimulation in vitro or ex vivo. Although this enhanced superoxide production correlates with effects due to the lethal toxin-induced blockade of ERK signaling, it requires JNK signaling that remains largely intact despite the activity of anthrax lethal toxin |
| 3.4.24.83 | anthrax lethal factor endopeptidase |
molecular biology |
Bacillus anthracis represses the immune response, in part by altering chromatin accessibility of IL-8 promoter to NFkappaB in epithelial cells. This epigenetic reprogramming, in addition to previously reported effects of lethal toxin, represents an efficient strategy used by Bacillus anthracis for invading the host |
| 3.4.24.83 | anthrax lethal factor endopeptidase |
molecular biology |
celastrol is identified as an inhibitor of lethal toxin-mediated macrophage lysis and suggests an inhibitory mechanism involving inhibition of the proteasome pathway |
| 3.4.24.83 | anthrax lethal factor endopeptidase |
molecular biology |
it is shown that treatment of RAW 264.7 murine macrophage cells with anthrax lethaltoxin induces autophagy suggesting a protective role as autophagy inhibition using 3-methyladenine results in an accelerated cell death |
| 3.4.24.83 | anthrax lethal factor endopeptidase |
molecular biology |
lethal toxin triggers the formation of a membrane-associated inflammasome complex in murine macrophages consisting of caspase-1 and Nalp1b, resulting in cleavage of cytosolic caspase-1 substrates and cell death |
| 3.4.24.83 | anthrax lethal factor endopeptidase |
molecular biology |
microarray analysis is used to investigate the effects of Bacillus anthracis lethal toxin on human neutrophil-like NB-4 cells to identify markers of intoxication. Genes down-regulated after a 2 h lethal toxin exposure include those encoding chemokines and transcription factors. Significant decreases in the mRNA of interleukin-8, CCL20, CCL3 and CCL4 are observed using real-time PCR. The decreases are more pronounced at 4 and 8 h and are lethal toxin-specific. Decreases in chemokine protein levels are evident after 24 h and are sensitive to low concentrations of lethal toxin. Co-incubation with an anti-lethal factor mAb restores levels of interleukin-8 to 100% and 50%, respectively |
| 3.4.24.83 | anthrax lethal factor endopeptidase |
molecular biology |
primary keratinocytes are resistant to LeTx cytotoxicity, and MEK cleavage does not correlate with LeTx cytotoxicity. LeTx is considered as an anti-inflammatory agent, however it upregulates RANTES |
| 3.4.24.83 | anthrax lethal factor endopeptidase |
molecular biology |
proteasome inhibitors block anthrax lethal toxin-mediated caspase-1 activation and can protect against cell death, indicating that the degradation of at least one cellular protein is required for cell death. Proteins can be degraded by the proteasome via the N-end rule. Using amino acid derivatives that act as inhibitors of this pathway, it is shown that the N-end rule is required for anthrax lethal toxin-mediated caspase-1 activation and cell death. The Streptomyces olivoreti peptide bestatin, which inhibits leucine, alanine and arginine aminopeptidases, protects macrophages against anthrax lethal toxin. c-IAP1, a mammalian member of the inhibitor of apoptosis protein (IAP) family is identified, as a novel N-end rule substrate degraded in macrophages treated with anthrax lethal toxin |
| 3.4.24.83 | anthrax lethal factor endopeptidase |
molecular biology |
protein expression profile of murine macrophages RAW264.7 treated with LeTx is analyzed using two-dimensional polyacrylamide gel electrophoresis and MALDI-TOF MS. Among the differentially expressed spots, cleaved mitogen-activated protein kinase kinase 1 acting as a negative element in the signal transduction pathway, and glucose-6-phosphate dehydrogenase playing a role in the protection of cells from hyperproduction of active oxygen are up-regulated LeTx-treated macrophages |
| 3.4.24.83 | anthrax lethal factor endopeptidase |
molecular biology |
results suggest that this toxin delivery system is capable of stimulating protective immune responses where effective immunization requires stimulation of both classes of T cells |
| 3.4.24.83 | anthrax lethal factor endopeptidase |
molecular biology |
the cellular damage inflicted by anthrax lethal toxin depends not only on the innate responses but also on the maturation stage of the cell, which modulates the more general caspase-1-independent responses |
| 3.4.24.83 | anthrax lethal factor endopeptidase |
molecular biology |
the effects of lethal toxin on the transcriptional regulation of the VCAM1 gene, which contains binding sites in its promoter region for NF-kappaB, IFN regulatory factor-1 (IRF-1), Sp1, GATA-2, and AP-1, in primary human endothelial cells is examined. Lethal toxin enhances cytokine-induced activation of NF-kappaB and IRF-1 which are key factors in the lethal toxin-mediated enhancement of TNF-induced VCAM-1 expression. Altering the activity of key transcription factors involved in host response to infection may be a critical mechanism by which lethal toxin contributes to anthrax pathogenesis |
| 3.4.24.83 | anthrax lethal factor endopeptidase |
molecular biology |
the in vitro effects of thermal stress on the killing of murine macrophages by anthrax lethal toxin are investigated. Heat shock rapidly halts anthrax lethal toxin-induced cell death without any impact on toxin uptake or mitogen-activated protein kinases cleavage, by a mechanism independent of novel protein synthesis, p38 activation, HSP90 activity or proteasome inhibition. Rather, heat shock prevents the activation of procaspase-1 in anthrax lethal toxin -treated cells, apparently by the sequestration of pro-caspase-1 in a large, inhibitory complex. Heat-shocked cell lysates strongly inhibit the active caspase-1 heterotetramer in vitro, independent of a specific inflammasome platform. Results suggest the presence of a cellular, heat shock-inducible, caspase-1 inhibiting factor |
| 3.4.24.83 | anthrax lethal factor endopeptidase |
molecular biology |
toxin effects of lethal toxin and edema toxin of Bacillus anthracis in bone marrow dendritic cells stimulated with either LPS or Legionella pneumophila are analysed. Lethal toxin, not ET, is more toxic for cells from BALB/c mice than from C57BL/6 as measured by 7-AAD uptake. Results support the conclusion that lethal toxin and edema toxin are not uniformly suppressive of dendritic cell function but rather modulate function up or down depending on variables such as the function tested, the microbial stimulus used, and the genetic variation in innate immune response mechanisms in the host cell |
| 3.4.24.86 | ADAM 17 endopeptidase |
molecular biology |
results indicate that oxygen regulates the expression of TACE and TACE may be important for placental development during human pregnancy |
| 3.4.24.86 | ADAM 17 endopeptidase |
molecular biology |
TACE may be involved in liver regeneration by pathway mediated with transforming growth factor-alpha-epidermal growth factor recptor in the cell-cycle progressive phase in vivo. TACE production and effect by paracrine may be a pathway of involvement in liver regeneration for the activated CD3+ T lymphocytes |
| 3.4.24.86 | ADAM 17 endopeptidase |
molecular biology |
TACE/ADAM17-like proteases might play a role in synaptic formation to generate specific neuronal connections by processing the excess amount of RA175/SynCAM1, a member of the immunoglobulin family 4, located in the non-synaptic region |
| 3.5.1.88 | peptide deformylase |
molecular biology |
the combination of plant peptide deformylase and peptide deformylase inhibitors may represent a native gene selectable marker system for chloroplast and nuclear transformation vectors |
 3.5.4.1 | cytosine deaminase |
molecular biology |
structure-based, computation-guided predictive method for reversibly controlling enzyme activity using covalently attached photo-responsive azobenzene groups. Application on yeast cytosine deaminase obtains an about 3fold change in enzyme activity by the photo-controlled modulation of the enzyme's active site lid structure, while fully maintaining thermostability. Multiple cycles of switching, controllable in real time, are possible |
| 3.5.4.16 | GTP cyclohydrolase I |
molecular biology |
mutations in Punch can act as genetic enhancers of Dube3a over-expression phenotypes |
| 3.5.4.16 | GTP cyclohydrolase I |
molecular biology |
mutations in Punch can act as genetic enhancers of Dube3a overexpression phenotypes |
| 3.5.4.23 | blasticidin-S deaminase |
molecular biology |
new selection marker for transformation of Arabidopsis thaliana and Nicotiana tabacum |
| 3.5.4.23 | blasticidin-S deaminase |
molecular biology |
BSD gene will be useful as a new dominant selectable marker for eukaryotes, first sucessful transformation with a drug resistance gene originating from a eukaryote by selecting for detoxification of the drug |
| 3.5.4.23 | blasticidin-S deaminase |
molecular biology |
generation of bicistronic expression vector mediating BSD resistance, blastidicin S selection of cells |
| 3.5.4.38 | single-stranded DNA cytosine deaminase |
molecular biology |
a target-AID base editor, designed to recruit cytidine deaminase (CDA) to the target DNA locus via the CRISPR/Cas9 system, can directly induce C to T mutation without double-strand breaks and donor DNA. This system is adopted in Yarrowia lipolytica for multiplex gene disruption. Target-specific gRNA(s) and a fusion protein consisting of a nickase Cas9, CDA1, and uracil DNA glycosylase inhibitor are expressed from a single plasmid to disrupt target genes by introducing a stop codon via C to T mutation within the mutational window. Using this Target-AID system, single gene disruption and simultaneous double gene disruption are achieved with the efficiencies up to 94% and 31%, respectively |
| 3.5.4.42 | N-isopropylammelide isopropylaminohydrolase |
molecular biology |
hybridization studies localize atzC together with TrzN and atzB to a 380-kb plasmid in Arthrobacter aurescens strain TC1 |
| 3.5.99.5 | 2-aminomuconate deaminase |
molecular biology |
nbzE, involved in the ring cleavage pathway of 2-aminophenol, is localized on the 6.6 kb SnaBI-SmaI fragment of the plasmid pNB1 and clusters in the order nbzC-nbzD-nbzE as an operon |
| 3.6.1.1 | inorganic diphosphatase |
molecular biology |
cycle sequencing methods |
| 3.6.4.B7 | RadA recombinase |
molecular biology |
genotyping of deep sea isolates and cutured deep-sea hydrothermal vent euryarchaeota 2 isolates using the enzyme sequence |
| 3.7.1.4 | phloretin hydrolase |
molecular biology |
98% similarity of the rabbit LPH precursor to PNGH sequence, LPH and PNGH enzymes have the same genomic origin, but differ in transcriptional and, possibly, post-translational processing |
| 3.7.1.4 | phloretin hydrolase |
molecular biology |
cell specificty of LPH gene expression depends upon both positive and negative interactions among elements in the first 2kb of the LPH 5'-flanking region, generally positive activity between -74 and -37 bp, a cell-specific negative region between -210 and -95 bp, and additional elements further toward the 5' terminus that confer a highly cell-specific response in reporter activity, potential binding sites for various intestinal transcription factors, binding of HNF3beta at three sites is relevant to LPH expression |
| 3.7.1.4 | phloretin hydrolase |
molecular biology |
LPH and PNGH enzymes have the same genomic origin, but differ in transcriptional and, possibly, post-translational processing |
| 3.7.1.7 | beta-diketone hydrolase |
molecular biology |
exhibits 63% identity with OPH of Pseudomonas sp. strain VM15C and 29-32% identity with the polyhydroxybutyrate depolymerases from Mesorhizobium loti, Rhizobium sp. and Sinorhizobium meliloti |
| 3.7.1.8 | 2,6-dioxo-6-phenylhexa-3-enoate hydrolase |
molecular biology |
open reading frame corresponding to the pcbD gene consists of 855 base pairs with an ATG initiation codon and a TGA termination codon, able to encode a polypeptide with a molecular weight of 31732 containing 284 amino acid residues, deduced amino acid sequence has 62% identity with those of the HOPDA hydrolases of Pseudomonas putida KF715, P. pseudoalcaligenes KF707, and Burkholderia cepacia LB400, and also significant homology with those of other hydrolytic enzymes including esterase, transferase, and peptidase |
| 3.7.1.8 | 2,6-dioxo-6-phenylhexa-3-enoate hydrolase |
molecular biology |
the deduced amino acid sequence of CarC shows 30.3, 31.3, and 31.8% identity with meta-cleavage compound hydrolases TodF, XylF, and DmpD, respectively, from other Pseudomonas |
| 3.7.1.8 | 2,6-dioxo-6-phenylhexa-3-enoate hydrolase |
molecular biology |
upstream of bphC are five ORFs, including bphD, exhibiting low homology with, and a different gene order from, previously characterized bph genes |
| 3.7.1.9 | 2-hydroxymuconate-6-semialdehyde hydrolase |
molecular biology |
orf234, encoding an alpha/beta hydrolase, which is distantly related to the meta-fission product hydrolases such as XylF, PhnD, and CumD |
| 3.7.1.9 | 2-hydroxymuconate-6-semialdehyde hydrolase |
molecular biology |
the Pseudomonas strutzeri OX1 genes coding for toluene and o-xylene catabolism are organized into at least two operons, the one coding for the phenol catabolism displays a gene order similar to that of the Pseudomonas sp. strain CF600dmp operon, includes HMSH, and is coregulated by the tou operon activator TouR |
