Rhodotorulapepsin: Difference between revisions

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Rhodotorulapepsin
Rhodotorulapepsin
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EC no.	3.4.23.26
CAS no.	37259-59-9
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Latest revision as of 05:49, 1 January 2024

Rhodotorulapepsin (EC 3.4.23.26, Rhodotorula aspartic proteinase, Cladosporium acid protease, Cladosporium acid proteinase, Cladosporium aspartic proteinase, Paecilomyces proteinase, Rhodotorula glutinis aspartic proteinase, Rhodotorula glutinis acid proteinase, Rhodotorula glutinis aspartic proteinase II, Rhodotorula acid proteinase) is an enzyme.^[1]^[2]^[3]^[4]^[5]^[6]^[7]^[8] This enzyme catalyses the following chemical reaction

Specificity similar to that of pepsin A. Cleaves Z-Lys-Ala-Ala-Ala and activates trypsinogen

This enzyme is present in yeast Rhodotorula glutinis.

References

^ Sawada, J. (1963). "Studies on the acid-protease of Paecilomyces varioti Bainier TPR-220. Part I. Crystallization of the acid-protease of Paecilomyces varioti Bainier TPR-220". Agric. Biol. Chem. 27: 677–683. doi:10.1080/00021369.1963.10858167.
^ Sawada, J. (1964). "The acid-protease of Paecilomyces varioti. III. The specificity of the crystalline acid-protease on synthetic substrates". Agric. Biol. Chem. 28: 869–875. doi:10.1080/00021369.1964.10858312.
^ Kamada M, Oda K, Murao S (1972). "The purification of the extracellular acid protease of Rhodotorula glutinis K-24 and its general properties". Agric. Biol. Chem. 36 (7): 1095–1101. doi:10.1271/bbb1961.36.1095.
^ Murao S, Funakoshi S, Oda K (1972). "Purification, crystallization and some enzymatic properties of acid protease of Cladosporium sp. No. 45-2". Agric. Biol. Chem. 36 (8): 1327–1333. doi:10.1271/bbb1961.36.1327.
^ Oda K, Kamada M, Murao S (1972). "Some physicochemical properties and substrate specificity of acid protease of Rhodotorula glutinis K-24". Agric. Biol. Chem. 36 (7): 1103–1108. doi:10.1271/bbb1961.36.1103.
^ Oda K, Funakoshi S, Murao S (1973). "Some physicochemical properties and substrate specificity of acid protease isolated from Cladosporium sp. No. 45-2". Agric. Biol. Chem. 37 (7): 1723–1729. doi:10.1271/bbb1961.37.1723.
^ Takahashi K, Chang WJ (September 1976). "The structure and function of acid proteases. V. Comparative studies on the specific inhibition of acid proteases by diazoacetyl-DL-norleucine methyl ester, 1,2-epoxy-3-(p-nitrophenoxy) propane and pepstatin". Journal of Biochemistry. 80 (3): 497–506. doi:10.1093/oxfordjournals.jbchem.a131304. PMID 10290.
^ Majima E, Oda K, Murao S, Ichishima E (1988). "Comparative study on the specificities of several fungal aspartic and acidic proteinases towards the tetradecapeptide of a renin substrate". Agric. Biol. Chem. 52 (3): 787–793. doi:10.1271/bbb1961.52.787.

External links

Rhodotorulapepsin at the U.S. National Library of Medicine Medical Subject Headings (MeSH)

[1] Sawada, J. (1963). "Studies on the acid-protease of Paecilomyces varioti Bainier TPR-220. Part I. Crystallization of the acid-protease of Paecilomyces varioti Bainier TPR-220". Agric. Biol. Chem. 27: 677–683. doi:10.1080/00021369.1963.10858167.

[2] Sawada, J. (1964). "The acid-protease of Paecilomyces varioti. III. The specificity of the crystalline acid-protease on synthetic substrates". Agric. Biol. Chem. 28: 869–875. doi:10.1080/00021369.1964.10858312.

[3] Kamada M, Oda K, Murao S (1972). "The purification of the extracellular acid protease of Rhodotorula glutinis K-24 and its general properties". Agric. Biol. Chem. 36 (7): 1095–1101. doi:10.1271/bbb1961.36.1095.

[4] Murao S, Funakoshi S, Oda K (1972). "Purification, crystallization and some enzymatic properties of acid protease of Cladosporium sp. No. 45-2". Agric. Biol. Chem. 36 (8): 1327–1333. doi:10.1271/bbb1961.36.1327.

[5] Oda K, Kamada M, Murao S (1972). "Some physicochemical properties and substrate specificity of acid protease of Rhodotorula glutinis K-24". Agric. Biol. Chem. 36 (7): 1103–1108. doi:10.1271/bbb1961.36.1103.

[6] Oda K, Funakoshi S, Murao S (1973). "Some physicochemical properties and substrate specificity of acid protease isolated from Cladosporium sp. No. 45-2". Agric. Biol. Chem. 37 (7): 1723–1729. doi:10.1271/bbb1961.37.1723.

[7] Takahashi K, Chang WJ (September 1976). "The structure and function of acid proteases. V. Comparative studies on the specific inhibition of acid proteases by diazoacetyl-DL-norleucine methyl ester, 1,2-epoxy-3-(p-nitrophenoxy) propane and pepstatin". Journal of Biochemistry. 80 (3): 497–506. doi:10.1093/oxfordjournals.jbchem.a131304. PMID 10290.

[8] Majima E, Oda K, Murao S, Ichishima E (1988). "Comparative study on the specificities of several fungal aspartic and acidic proteinases towards the tetradecapeptide of a renin substrate". Agric. Biol. Chem. 52 (3): 787–793. doi:10.1271/bbb1961.52.787.

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@@ Line 1: / Line 1: @@
+{{Short description|Enzyme}}
 {{Infobox enzyme
-| Name = Rhodotorulapepsin
+| Name       = Rhodotorulapepsin
-| EC_number = 3.4.23.26
+| EC_number  = 3.4.23.26
 | CAS_number = 37259-59-9
+| GO_code    =
-| IUBMB_EC_number = 3/4/23/26
-| GO_code =
+| image      =
-| image =
+| width      =
-| width =
+| caption    =
-| caption =
 }}
-'''Rhodotorulapepsin''' ({{EC number|3.4.23.26}}, ''Rhodotorula aspartic proteinase'', ''Cladosporium acid protease'', ''Cladosporium acid proteinase'', ''Cladosporium aspartic proteinase'', ''Paecilomyces proteinase'', ''Rhodotorula glutinis aspartic proteinase'', ''Rhodotorula glutinis acid proteinase'', ''Rhodotorula glutinis aspartic proteinase II'', ''Rhodotorula acid proteinase'') is an [[enzyme]].<ref>{{cite journal | title = Studies on the acid-protease of ''Paecilomyces varioti'' Bainier TPR-220. Part I. Crystallization of the acid-protease of Paecilomyces varioti Bainier TPR-220 |author = Sawada, J. |journal = Agric. Biol. Chem. |date = 1963 |volume = 27 |pages = 677–683 |pmid = | doi = 10.1080/00021369.1963.10858167}}</ref><ref>{{cite journal | title = The acid-protease of ''Paecilomyces varioti''. III. The specificity of the crystalline acid-protease on synthetic substrates |author = Sawada, J. |journal = Agric. Biol. Chem. |date = 1964 |volume = 28 |pages = 869–875 |pmid = | doi = 10.1080/00021369.1964.10858312}}</ref><ref>{{cite journal | title = The purification of the extracellular acid protease of ''Rhodotorula glutinis'' K-24 and its general properties | vauthors = Kamada M, Oda K, Murao S |journal = Agric. Biol. Chem. |date = 1972 |volume = 36 |pages = 1095–1101 |pmid = |doi=10.1271/bbb1961.36.1095|doi-access = free }}</ref><ref>{{cite journal | title = Purification, crystallization and some enzymatic properties of acid protease of ''Cladosporium'' sp. No. 45-2 | vauthors = Murao S, Funakoshi S, Oda K |journal = Agric. Biol. Chem. |date = 1972 |volume = 36 |pages = 1327–1333 |pmid = |doi=10.1271/bbb1961.36.1327|doi-access = free }}</ref><ref>{{cite journal | title = Some physicochemical properties and substrate specificity of acid protease of ''Rhodotorula glutinis'' K-24 | vauthors = Oda K, Kamada M, Murao S |journal = Agric. Biol. Chem. |date = 1972 |volume = 36 |pages = 1103–1108 |pmid = |doi=10.1271/bbb1961.36.1103|doi-access = free }}</ref><ref>{{cite journal | title = Some physicochemical properties and substrate specificity of acid protease isolated from ''Cladosporium'' sp. No. 45-2 | vauthors = Oda K, Funakoshi S, Murao S |journal = Agric. Biol. Chem. |date = 1973 |volume = 37 |pages = 1723–1729 |pmid = |doi=10.1271/bbb1961.37.1723|doi-access = free }}</ref><ref>{{cite journal | vauthors = Takahashi K, Chang WJ | title = The structure and function of acid proteases. V. Comparative studies on the specific inhibition of acid proteases by diazoacetyl-DL-norleucine methyl ester, 1,2-epoxy-3-(p-nitrophenoxy) propane and pepstatin | journal = Journal of Biochemistry | volume = 80 | issue = 3 | pages = 497–506 | date = September 1976 | pmid = 10290 }}</ref><ref>{{cite journal | title = Comparative study on the specificities of several fungal aspartic and acidic proteinases towards the tetradecapeptide of a renin substrate | vauthors = Majima E, Oda K, Murao S, Ichishima E |journal = Agric. Biol. Chem. |date = 1988 |volume = 52 |pages = 787–793 |pmid = |doi=10.1271/bbb1961.52.787|doi-access = free }}</ref> This enzyme [[catalysis|catalyses]] the following [[chemical reaction]]
+'''Rhodotorulapepsin''' ({{EC number|3.4.23.26}}, ''Rhodotorula aspartic proteinase'', ''Cladosporium acid protease'', ''Cladosporium acid proteinase'', ''Cladosporium aspartic proteinase'', ''Paecilomyces proteinase'', ''Rhodotorula glutinis aspartic proteinase'', ''Rhodotorula glutinis acid proteinase'', ''Rhodotorula glutinis aspartic proteinase II'', ''Rhodotorula acid proteinase'') is an [[enzyme]].<ref>{{cite journal | title = Studies on the acid-protease of ''Paecilomyces varioti'' Bainier TPR-220. Part I. Crystallization of the acid-protease of Paecilomyces varioti Bainier TPR-220 |author = Sawada, J. |journal = Agric. Biol. Chem. |date = 1963 |volume = 27 |pages = 677–683 | doi = 10.1080/00021369.1963.10858167}}</ref><ref>{{cite journal | title = The acid-protease of ''Paecilomyces varioti''. III. The specificity of the crystalline acid-protease on synthetic substrates |author = Sawada, J. |journal = Agric. Biol. Chem. |date = 1964 |volume = 28 |pages = 869–875 | doi = 10.1080/00021369.1964.10858312}}</ref><ref>{{cite journal | title = The purification of the extracellular acid protease of ''Rhodotorula glutinis'' K-24 and its general properties | vauthors = Kamada M, Oda K, Murao S |journal = Agric. Biol. Chem. |date = 1972 |volume = 36 | issue = 7 |pages = 1095–1101 |doi=10.1271/bbb1961.36.1095|doi-access = free }}</ref><ref>{{cite journal | title = Purification, crystallization and some enzymatic properties of acid protease of ''Cladosporium'' sp. No. 45-2 | vauthors = Murao S, Funakoshi S, Oda K |journal = Agric. Biol. Chem. |date = 1972 |volume = 36 | issue = 8 |pages = 1327–1333 |doi=10.1271/bbb1961.36.1327|doi-access = free }}</ref><ref>{{cite journal | title = Some physicochemical properties and substrate specificity of acid protease of ''Rhodotorula glutinis'' K-24 | vauthors = Oda K, Kamada M, Murao S |journal = Agric. Biol. Chem. |date = 1972 |volume = 36 | issue = 7 |pages = 1103–1108 |doi=10.1271/bbb1961.36.1103|doi-access = free }}</ref><ref>{{cite journal | title = Some physicochemical properties and substrate specificity of acid protease isolated from ''Cladosporium'' sp. No. 45-2 | vauthors = Oda K, Funakoshi S, Murao S |journal = Agric. Biol. Chem. |date = 1973 |volume = 37 | issue = 7 |pages = 1723–1729 |doi=10.1271/bbb1961.37.1723|doi-access = free }}</ref><ref>{{cite journal | vauthors = Takahashi K, Chang WJ | title = The structure and function of acid proteases. V. Comparative studies on the specific inhibition of acid proteases by diazoacetyl-DL-norleucine methyl ester, 1,2-epoxy-3-(p-nitrophenoxy) propane and pepstatin | journal = Journal of Biochemistry | volume = 80 | issue = 3 | pages = 497–506 | date = September 1976 | doi = 10.1093/oxfordjournals.jbchem.a131304 | pmid = 10290 }}</ref><ref>{{cite journal | title = Comparative study on the specificities of several fungal aspartic and acidic proteinases towards the tetradecapeptide of a renin substrate | vauthors = Majima E, Oda K, Murao S, Ichishima E |journal = Agric. Biol. Chem. |date = 1988 |volume = 52 | issue = 3 |pages = 787–793 |doi=10.1271/bbb1961.52.787|doi-access = free }}</ref> This enzyme [[catalysis|catalyses]] the following [[chemical reaction]]
 : Specificity similar to that of [[pepsin A]]. Cleaves Z-Lys-Ala-Ala-Ala and activates [[trypsinogen]]

v t e Proteases: aspartate proteases (EC 3.4.23)
Vertebrate	Pepsin Chymosin Renin Signal peptide peptidase Beta secretase 1 2
Pathogenic	Plasmepsin HIV-1 protease
Plant	Nepenthesin
Cathepsin	D E

v t e Enzymes
Activity	Active site Binding site Catalytic triad Oxyanion hole Enzyme promiscuity Diffusion-limited enzyme Cofactor Enzyme catalysis
Regulation	Allosteric regulation Cooperativity Enzyme inhibitor Enzyme activator
Classification	EC number Enzyme superfamily Enzyme family List of enzymes
Kinetics	Enzyme kinetics Eadie–Hofstee diagram Hanes–Woolf plot Lineweaver–Burk plot Michaelis–Menten kinetics
Types	EC1 Oxidoreductases (list) EC2 Transferases (list) EC3 Hydrolases (list) EC4 Lyases (list) EC5 Isomerases (list) EC6 Ligases (list) EC7 Translocases (list)