BRENDA - Enzyme Database
show all sequences of 3.4.17.23

Structure analysis of the receptor binding of 2019-nCoV

Chen, Y.; Guo, Y.; Pan, Y.; Zhao, Z.; Biochem. Biophys. Res. Commun. FEHLT, 0000 (2020)

Data extracted from this reference:

Application
Application
Commentary
Organism
medicine
antibodies and small molecular inhibitors that can block the interaction of the enzyme (ACE2) with the receptor binding domain can to combat the virus SARS-CoV-2
Homo sapiens
Organism
Organism
UniProt
Commentary
Textmining
Callorhinchus milii
XP_007889845.1
-
-
Homo sapiens
Q9BYF1
-
-
Nipponia nippon
A0A091UR55
-
-
Paguma larvata
Q56NL1
-
-
Protobothrops mucrosquamatus
XP_029140508.1
-
-
Rhinolophus sinicus
E2DHI7
-
-
Xenopus laevis
XP_018104311.1
-
-
Source Tissue
Source Tissue
Commentary
Organism
Textmining
intestine
predominantly expressed in intestines, testis, and kidney
Homo sapiens
-
kidney
predominantly expressed in intestines, testis, and kidney
Homo sapiens
-
lung
expression level of ACE2 in the lung is minimal
Homo sapiens
-
testis
predominantly expressed in intestines, testis, and kidney
Homo sapiens
-
Synonyms
Synonyms
Commentary
Organism
ACE2
-
Callorhinchus milii
ACE2
-
Nipponia nippon
ACE2
-
Protobothrops mucrosquamatus
ACE2
-
Rhinolophus sinicus
ACE2
-
Xenopus laevis
ACE2
-
Paguma larvata
ACE2
-
Homo sapiens
Application (protein specific)
Application
Commentary
Organism
medicine
antibodies and small molecular inhibitors that can block the interaction of the enzyme (ACE2) with the receptor binding domain can to combat the virus SARS-CoV-2
Homo sapiens
Source Tissue (protein specific)
Source Tissue
Commentary
Organism
Textmining
intestine
predominantly expressed in intestines, testis, and kidney
Homo sapiens
-
kidney
predominantly expressed in intestines, testis, and kidney
Homo sapiens
-
lung
expression level of ACE2 in the lung is minimal
Homo sapiens
-
testis
predominantly expressed in intestines, testis, and kidney
Homo sapiens
-
General Information
General Information
Commentary
Organism
drug target
antibodies and small molecular inhibitors that can block the interaction of the enzyme (ACE2) with the receptor binding domain can to combat the virus SARS-CoV-2
Homo sapiens
evolution
ACE2 is widely expressed in the animal kingdom from fish, amphibians, reptiles, birds, to mammals. Remarkably, its structure is highly conserved. Comparison of human ACE2 with that of a civet (Paguma larvata), a bat (Rhinolophus sinicus), a bird (Nipponia nippon), a snake (Protobothrops mucrosquamatus), a frog (Xenopus laevis), and a fish (Callorhinchus milii) reveal amino acid sequence identity of 83%, 81%, 83%, 61%, 60%, and 59%, respectively
Callorhinchus milii
evolution
ACE2 is widely expressed in the animal kingdom from fish, amphibians, reptiles, birds, to mammals. Remarkably, its structure is highly conserved. Comparison of human ACE2 with that of a civet (Paguma larvata), a bat (Rhinolophus sinicus), a bird (Nipponia nippon), a snake (Protobothrops mucrosquamatus), a frog (Xenopus laevis), and a fish (Callorhinchus milii) reveal amino acid sequence identity of 83%, 81%, 83%, 61%, 60%, and 59%, respectively
Homo sapiens
evolution
ACE2 is widely expressed in the animal kingdom from fish, amphibians, reptiles, birds, to mammals. Remarkably, its structure is highly conserved. Comparison of human ACE2 with that of a civet (Paguma larvata), a bat (Rhinolophus sinicus), a bird (Nipponia nippon), a snake (Protobothrops mucrosquamatus), a frog (Xenopus laevis), and a fish (Callorhinchus milii) reveal amino acid sequence identity of 83%, 81%, 83%, 61%, 60%, and 59%, respectively
Nipponia nippon
evolution
ACE2 is widely expressed in the animal kingdom from fish, amphibians, reptiles, birds, to mammals. Remarkably, its structure is highly conserved. Comparison of human ACE2 with that of a civet (Paguma larvata), a bat (Rhinolophus sinicus), a bird (Nipponia nippon), a snake (Protobothrops mucrosquamatus), a frog (Xenopus laevis), and a fish (Callorhinchus milii) reveal amino acid sequence identity of 83%, 81%, 83%, 61%, 60%, and 59%, respectively
Paguma larvata
evolution
ACE2 is widely expressed in the animal kingdom from fish, amphibians, reptiles, birds, to mammals. Remarkably, its structure is highly conserved. Comparison of human ACE2 with that of a civet (Paguma larvata), a bat (Rhinolophus sinicus), a bird (Nipponia nippon), a snake (Protobothrops mucrosquamatus), a frog (Xenopus laevis), and a fish (Callorhinchus milii) reveal amino acid sequence identity of 83%, 81%, 83%, 61%, 60%, and 59%, respectively
Protobothrops mucrosquamatus
evolution
ACE2 is widely expressed in the animal kingdom from fish, amphibians, reptiles, birds, to mammals. Remarkably, its structure is highly conserved. Comparison of human ACE2 with that of a civet (Paguma larvata), a bat (Rhinolophus sinicus), a bird (Nipponia nippon), a snake (Protobothrops mucrosquamatus), a frog (Xenopus laevis), and a fish (Callorhinchus milii) reveal amino acid sequence identity of 83%, 81%, 83%, 61%, 60%, and 59%, respectively
Rhinolophus sinicus
evolution
ACE2 is widely expressed in the animal kingdom from fish, amphibians, reptiles, birds, to mammals. Remarkably, its structure is highly conserved. Comparison of human ACE2 with that of a civet (Paguma larvata), a bat (Rhinolophus sinicus), a bird (Nipponia nippon), a snake (Protobothrops mucrosquamatus), a frog (Xenopus laevis), and a fish (Callorhinchus milii) reveal amino acid sequence identity of 83%, 81%, 83%, 61%, 60%, and 59%, respectively
Xenopus laevis
physiological function
the receptor binding domain (RBD) of spike glycoprotein is responsible for entry of coronaviruses (SARS-CoV-2 and SARS-CoV) into host cells. The RBDs from the two viruses share 72% identity in amino acid sequences, and molecular simulation reveals highly similar ternary structures. Severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) has a distinct loop with flexible glycyl residues replacing rigid prolyl residues in SARS-CoV. Molecular modeling reveals that SARS-CoV-2 RBD has a stronger interaction with angiotensin converting enzyme 2 (ACE2). A unique phenylalanine F486 in the flexible loop likely plays a major role because its penetration into a deep hydrophobic pocket in ACE2. ACE2 is widely expressed with conserved primary structures throughout the animal kingdom from fish, amphibians, reptiles, birds, to mammals. Structural analysis suggests that ACE2 from these animals can potentially bind RBD of SARS-CoV-2, making them all possible natural hosts for the virus
Callorhinchus milii
physiological function
the receptor binding domain (RBD) of spike glycoprotein is responsible for entry of coronaviruses (SARS-CoV-2 and SARS-CoV) into host cells. The RBDs from the two viruses share 72% identity in amino acid sequences, and molecular simulation reveals highly similar ternary structures. Severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) has a distinct loop with flexible glycyl residues replacing rigid prolyl residues in SARS-CoV. Molecular modeling reveals that SARS-CoV-2 RBD has a stronger interaction with angiotensin converting enzyme 2 (ACE2). A unique phenylalanine F486 in the flexible loop likely plays a major role because its penetration into a deep hydrophobic pocket in ACE2. ACE2 is widely expressed with conserved primary structures throughout the animal kingdom from fish, amphibians, reptiles, birds, to mammals. Structural analysis suggests that ACE2 from these animals can potentially bind RBD of SARS-CoV-2, making them all possible natural hosts for the virus
Homo sapiens
physiological function
the receptor binding domain (RBD) of spike glycoprotein is responsible for entry of coronaviruses (SARS-CoV-2 and SARS-CoV) into host cells. The RBDs from the two viruses share 72% identity in amino acid sequences, and molecular simulation reveals highly similar ternary structures. Severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) has a distinct loop with flexible glycyl residues replacing rigid prolyl residues in SARS-CoV. Molecular modeling reveals that SARS-CoV-2 RBD has a stronger interaction with angiotensin converting enzyme 2 (ACE2). A unique phenylalanine F486 in the flexible loop likely plays a major role because its penetration into a deep hydrophobic pocket in ACE2. ACE2 is widely expressed with conserved primary structures throughout the animal kingdom from fish, amphibians, reptiles, birds, to mammals. Structural analysis suggests that ACE2 from these animals can potentially bind RBD of SARS-CoV-2, making them all possible natural hosts for the virus
Nipponia nippon
physiological function
the receptor binding domain (RBD) of spike glycoprotein is responsible for entry of coronaviruses (SARS-CoV-2 and SARS-CoV) into host cells. The RBDs from the two viruses share 72% identity in amino acid sequences, and molecular simulation reveals highly similar ternary structures. Severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) has a distinct loop with flexible glycyl residues replacing rigid prolyl residues in SARS-CoV. Molecular modeling reveals that SARS-CoV-2 RBD has a stronger interaction with angiotensin converting enzyme 2 (ACE2). A unique phenylalanine F486 in the flexible loop likely plays a major role because its penetration into a deep hydrophobic pocket in ACE2. ACE2 is widely expressed with conserved primary structures throughout the animal kingdom from fish, amphibians, reptiles, birds, to mammals. Structural analysis suggests that ACE2 from these animals can potentially bind RBD of SARS-CoV-2, making them all possible natural hosts for the virus
Paguma larvata
physiological function
the receptor binding domain (RBD) of spike glycoprotein is responsible for entry of coronaviruses (SARS-CoV-2 and SARS-CoV) into host cells. The RBDs from the two viruses share 72% identity in amino acid sequences, and molecular simulation reveals highly similar ternary structures. Severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) has a distinct loop with flexible glycyl residues replacing rigid prolyl residues in SARS-CoV. Molecular modeling reveals that SARS-CoV-2 RBD has a stronger interaction with angiotensin converting enzyme 2 (ACE2). A unique phenylalanine F486 in the flexible loop likely plays a major role because its penetration into a deep hydrophobic pocket in ACE2. ACE2 is widely expressed with conserved primary structures throughout the animal kingdom from fish, amphibians, reptiles, birds, to mammals. Structural analysis suggests that ACE2 from these animals can potentially bind RBD of SARS-CoV-2, making them all possible natural hosts for the virus
Protobothrops mucrosquamatus
physiological function
the receptor binding domain (RBD) of spike glycoprotein is responsible for entry of coronaviruses (SARS-CoV-2 and SARS-CoV) into host cells. The RBDs from the two viruses share 72% identity in amino acid sequences, and molecular simulation reveals highly similar ternary structures. Severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) has a distinct loop with flexible glycyl residues replacing rigid prolyl residues in SARS-CoV. Molecular modeling reveals that SARS-CoV-2 RBD has a stronger interaction with angiotensin converting enzyme 2 (ACE2). A unique phenylalanine F486 in the flexible loop likely plays a major role because its penetration into a deep hydrophobic pocket in ACE2. ACE2 is widely expressed with conserved primary structures throughout the animal kingdom from fish, amphibians, reptiles, birds, to mammals. Structural analysis suggests that ACE2 from these animals can potentially bind RBD of SARS-CoV-2, making them all possible natural hosts for the virus
Rhinolophus sinicus
physiological function
the receptor binding domain (RBD) of spike glycoprotein is responsible for entry of coronaviruses (SARS-CoV-2 and SARS-CoV) into host cells. The RBDs from the two viruses share 72% identity in amino acid sequences, and molecular simulation reveals highly similar ternary structures. Severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) has a distinct loop with flexible glycyl residues replacing rigid prolyl residues in SARS-CoV. Molecular modeling reveals that SARS-CoV-2 RBD has a stronger interaction with angiotensin converting enzyme 2 (ACE2). A unique phenylalanine F486 in the flexible loop likely plays a major role because its penetration into a deep hydrophobic pocket in ACE2. ACE2 is widely expressed with conserved primary structures throughout the animal kingdom from fish, amphibians, reptiles, birds, to mammals. Structural analysis suggests that ACE2 from these animals can potentially bind RBD of SARS-CoV-2, making them all possible natural hosts for the virus
Xenopus laevis
General Information (protein specific)
General Information
Commentary
Organism
drug target
antibodies and small molecular inhibitors that can block the interaction of the enzyme (ACE2) with the receptor binding domain can to combat the virus SARS-CoV-2
Homo sapiens
evolution
ACE2 is widely expressed in the animal kingdom from fish, amphibians, reptiles, birds, to mammals. Remarkably, its structure is highly conserved. Comparison of human ACE2 with that of a civet (Paguma larvata), a bat (Rhinolophus sinicus), a bird (Nipponia nippon), a snake (Protobothrops mucrosquamatus), a frog (Xenopus laevis), and a fish (Callorhinchus milii) reveal amino acid sequence identity of 83%, 81%, 83%, 61%, 60%, and 59%, respectively
Callorhinchus milii
evolution
ACE2 is widely expressed in the animal kingdom from fish, amphibians, reptiles, birds, to mammals. Remarkably, its structure is highly conserved. Comparison of human ACE2 with that of a civet (Paguma larvata), a bat (Rhinolophus sinicus), a bird (Nipponia nippon), a snake (Protobothrops mucrosquamatus), a frog (Xenopus laevis), and a fish (Callorhinchus milii) reveal amino acid sequence identity of 83%, 81%, 83%, 61%, 60%, and 59%, respectively
Homo sapiens
evolution
ACE2 is widely expressed in the animal kingdom from fish, amphibians, reptiles, birds, to mammals. Remarkably, its structure is highly conserved. Comparison of human ACE2 with that of a civet (Paguma larvata), a bat (Rhinolophus sinicus), a bird (Nipponia nippon), a snake (Protobothrops mucrosquamatus), a frog (Xenopus laevis), and a fish (Callorhinchus milii) reveal amino acid sequence identity of 83%, 81%, 83%, 61%, 60%, and 59%, respectively
Nipponia nippon
evolution
ACE2 is widely expressed in the animal kingdom from fish, amphibians, reptiles, birds, to mammals. Remarkably, its structure is highly conserved. Comparison of human ACE2 with that of a civet (Paguma larvata), a bat (Rhinolophus sinicus), a bird (Nipponia nippon), a snake (Protobothrops mucrosquamatus), a frog (Xenopus laevis), and a fish (Callorhinchus milii) reveal amino acid sequence identity of 83%, 81%, 83%, 61%, 60%, and 59%, respectively
Paguma larvata
evolution
ACE2 is widely expressed in the animal kingdom from fish, amphibians, reptiles, birds, to mammals. Remarkably, its structure is highly conserved. Comparison of human ACE2 with that of a civet (Paguma larvata), a bat (Rhinolophus sinicus), a bird (Nipponia nippon), a snake (Protobothrops mucrosquamatus), a frog (Xenopus laevis), and a fish (Callorhinchus milii) reveal amino acid sequence identity of 83%, 81%, 83%, 61%, 60%, and 59%, respectively
Protobothrops mucrosquamatus
evolution
ACE2 is widely expressed in the animal kingdom from fish, amphibians, reptiles, birds, to mammals. Remarkably, its structure is highly conserved. Comparison of human ACE2 with that of a civet (Paguma larvata), a bat (Rhinolophus sinicus), a bird (Nipponia nippon), a snake (Protobothrops mucrosquamatus), a frog (Xenopus laevis), and a fish (Callorhinchus milii) reveal amino acid sequence identity of 83%, 81%, 83%, 61%, 60%, and 59%, respectively
Rhinolophus sinicus
evolution
ACE2 is widely expressed in the animal kingdom from fish, amphibians, reptiles, birds, to mammals. Remarkably, its structure is highly conserved. Comparison of human ACE2 with that of a civet (Paguma larvata), a bat (Rhinolophus sinicus), a bird (Nipponia nippon), a snake (Protobothrops mucrosquamatus), a frog (Xenopus laevis), and a fish (Callorhinchus milii) reveal amino acid sequence identity of 83%, 81%, 83%, 61%, 60%, and 59%, respectively
Xenopus laevis
physiological function
the receptor binding domain (RBD) of spike glycoprotein is responsible for entry of coronaviruses (SARS-CoV-2 and SARS-CoV) into host cells. The RBDs from the two viruses share 72% identity in amino acid sequences, and molecular simulation reveals highly similar ternary structures. Severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) has a distinct loop with flexible glycyl residues replacing rigid prolyl residues in SARS-CoV. Molecular modeling reveals that SARS-CoV-2 RBD has a stronger interaction with angiotensin converting enzyme 2 (ACE2). A unique phenylalanine F486 in the flexible loop likely plays a major role because its penetration into a deep hydrophobic pocket in ACE2. ACE2 is widely expressed with conserved primary structures throughout the animal kingdom from fish, amphibians, reptiles, birds, to mammals. Structural analysis suggests that ACE2 from these animals can potentially bind RBD of SARS-CoV-2, making them all possible natural hosts for the virus
Callorhinchus milii
physiological function
the receptor binding domain (RBD) of spike glycoprotein is responsible for entry of coronaviruses (SARS-CoV-2 and SARS-CoV) into host cells. The RBDs from the two viruses share 72% identity in amino acid sequences, and molecular simulation reveals highly similar ternary structures. Severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) has a distinct loop with flexible glycyl residues replacing rigid prolyl residues in SARS-CoV. Molecular modeling reveals that SARS-CoV-2 RBD has a stronger interaction with angiotensin converting enzyme 2 (ACE2). A unique phenylalanine F486 in the flexible loop likely plays a major role because its penetration into a deep hydrophobic pocket in ACE2. ACE2 is widely expressed with conserved primary structures throughout the animal kingdom from fish, amphibians, reptiles, birds, to mammals. Structural analysis suggests that ACE2 from these animals can potentially bind RBD of SARS-CoV-2, making them all possible natural hosts for the virus
Homo sapiens
physiological function
the receptor binding domain (RBD) of spike glycoprotein is responsible for entry of coronaviruses (SARS-CoV-2 and SARS-CoV) into host cells. The RBDs from the two viruses share 72% identity in amino acid sequences, and molecular simulation reveals highly similar ternary structures. Severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) has a distinct loop with flexible glycyl residues replacing rigid prolyl residues in SARS-CoV. Molecular modeling reveals that SARS-CoV-2 RBD has a stronger interaction with angiotensin converting enzyme 2 (ACE2). A unique phenylalanine F486 in the flexible loop likely plays a major role because its penetration into a deep hydrophobic pocket in ACE2. ACE2 is widely expressed with conserved primary structures throughout the animal kingdom from fish, amphibians, reptiles, birds, to mammals. Structural analysis suggests that ACE2 from these animals can potentially bind RBD of SARS-CoV-2, making them all possible natural hosts for the virus
Nipponia nippon
physiological function
the receptor binding domain (RBD) of spike glycoprotein is responsible for entry of coronaviruses (SARS-CoV-2 and SARS-CoV) into host cells. The RBDs from the two viruses share 72% identity in amino acid sequences, and molecular simulation reveals highly similar ternary structures. Severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) has a distinct loop with flexible glycyl residues replacing rigid prolyl residues in SARS-CoV. Molecular modeling reveals that SARS-CoV-2 RBD has a stronger interaction with angiotensin converting enzyme 2 (ACE2). A unique phenylalanine F486 in the flexible loop likely plays a major role because its penetration into a deep hydrophobic pocket in ACE2. ACE2 is widely expressed with conserved primary structures throughout the animal kingdom from fish, amphibians, reptiles, birds, to mammals. Structural analysis suggests that ACE2 from these animals can potentially bind RBD of SARS-CoV-2, making them all possible natural hosts for the virus
Paguma larvata
physiological function
the receptor binding domain (RBD) of spike glycoprotein is responsible for entry of coronaviruses (SARS-CoV-2 and SARS-CoV) into host cells. The RBDs from the two viruses share 72% identity in amino acid sequences, and molecular simulation reveals highly similar ternary structures. Severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) has a distinct loop with flexible glycyl residues replacing rigid prolyl residues in SARS-CoV. Molecular modeling reveals that SARS-CoV-2 RBD has a stronger interaction with angiotensin converting enzyme 2 (ACE2). A unique phenylalanine F486 in the flexible loop likely plays a major role because its penetration into a deep hydrophobic pocket in ACE2. ACE2 is widely expressed with conserved primary structures throughout the animal kingdom from fish, amphibians, reptiles, birds, to mammals. Structural analysis suggests that ACE2 from these animals can potentially bind RBD of SARS-CoV-2, making them all possible natural hosts for the virus
Protobothrops mucrosquamatus
physiological function
the receptor binding domain (RBD) of spike glycoprotein is responsible for entry of coronaviruses (SARS-CoV-2 and SARS-CoV) into host cells. The RBDs from the two viruses share 72% identity in amino acid sequences, and molecular simulation reveals highly similar ternary structures. Severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) has a distinct loop with flexible glycyl residues replacing rigid prolyl residues in SARS-CoV. Molecular modeling reveals that SARS-CoV-2 RBD has a stronger interaction with angiotensin converting enzyme 2 (ACE2). A unique phenylalanine F486 in the flexible loop likely plays a major role because its penetration into a deep hydrophobic pocket in ACE2. ACE2 is widely expressed with conserved primary structures throughout the animal kingdom from fish, amphibians, reptiles, birds, to mammals. Structural analysis suggests that ACE2 from these animals can potentially bind RBD of SARS-CoV-2, making them all possible natural hosts for the virus
Rhinolophus sinicus
physiological function
the receptor binding domain (RBD) of spike glycoprotein is responsible for entry of coronaviruses (SARS-CoV-2 and SARS-CoV) into host cells. The RBDs from the two viruses share 72% identity in amino acid sequences, and molecular simulation reveals highly similar ternary structures. Severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) has a distinct loop with flexible glycyl residues replacing rigid prolyl residues in SARS-CoV. Molecular modeling reveals that SARS-CoV-2 RBD has a stronger interaction with angiotensin converting enzyme 2 (ACE2). A unique phenylalanine F486 in the flexible loop likely plays a major role because its penetration into a deep hydrophobic pocket in ACE2. ACE2 is widely expressed with conserved primary structures throughout the animal kingdom from fish, amphibians, reptiles, birds, to mammals. Structural analysis suggests that ACE2 from these animals can potentially bind RBD of SARS-CoV-2, making them all possible natural hosts for the virus
Xenopus laevis
Other publictions for EC 3.4.17.23
No.
1st author
Pub Med
title
organims
journal
volume
pages
year
Activating Compound
Application
Cloned(Commentary)
Crystallization (Commentary)
Engineering
General Stability
Inhibitors
KM Value [mM]
Localization
Metals/Ions
Molecular Weight [Da]
Natural Substrates/ Products (Substrates)
Organic Solvent Stability
Organism
Oxidation Stability
Posttranslational Modification
Purification (Commentary)
Reaction
Renatured (Commentary)
Source Tissue
Specific Activity [micromol/min/mg]
Storage Stability
Substrates and Products (Substrate)
Subunits
Synonyms
Temperature Optimum [°C]
Temperature Range [°C]
Temperature Stability [°C]
Turnover Number [1/s]
pH Optimum
pH Range
pH Stability
Cofactor
Ki Value [mM]
pI Value
IC50 Value
Activating Compound (protein specific)
Application (protein specific)
Cloned(Commentary) (protein specific)
Cofactor (protein specific)
Crystallization (Commentary) (protein specific)
Engineering (protein specific)
General Stability (protein specific)
IC50 Value (protein specific)
Inhibitors (protein specific)
Ki Value [mM] (protein specific)
KM Value [mM] (protein specific)
Localization (protein specific)
Metals/Ions (protein specific)
Molecular Weight [Da] (protein specific)
Natural Substrates/ Products (Substrates) (protein specific)
Organic Solvent Stability (protein specific)
Oxidation Stability (protein specific)
Posttranslational Modification (protein specific)
Purification (Commentary) (protein specific)
Renatured (Commentary) (protein specific)
Source Tissue (protein specific)
Specific Activity [micromol/min/mg] (protein specific)
Storage Stability (protein specific)
Substrates and Products (Substrate) (protein specific)
Subunits (protein specific)
Temperature Optimum [°C] (protein specific)
Temperature Range [°C] (protein specific)
Temperature Stability [°C] (protein specific)
Turnover Number [1/s] (protein specific)
pH Optimum (protein specific)
pH Range (protein specific)
pH Stability (protein specific)
pI Value (protein specific)
Expression
General Information
General Information (protein specific)
Expression (protein specific)
KCat/KM [mM/s]
KCat/KM [mM/s] (protein specific)