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出典(authority):フリー百科事典『ウィキペディア（Wikipedia）』「2016/04/07 04:33:12」(JST)
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| Glutamate carboxypeptidase |
| Identifiers |
| EC number |
3.4.17.11 |
| CAS number |
9074-87-7 |
| Databases |
| IntEnz |
IntEnz view |
| BRENDA |
BRENDA entry |
| ExPASy |
NiceZyme view |
| KEGG |
KEGG entry |
| MetaCyc |
metabolic pathway |
| PRIAM |
profile |
| PDB structures |
RCSB PDB PDBe PDBsum |
| Search |
| PMC |
articles |
| PubMed |
articles |
| NCBI |
proteins |
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Glutamate carboxypeptidase (EC 3.4.17.11, carboxypeptidase G, carboxypeptidase G1, carboxypeptidase G2, glutamyl carboxypeptidase, N-pteroyl-L-glutamate hydrolase) is an enzyme.[1][2][3][4] This enzyme catalyses the following chemical reaction
- Release of C-terminal glutamate residues from a wide range of N-acylating moieties, including peptidyl, aminoacyl, benzoyl, benzyloxycarbonyl, folyl and pteroyl groups
This zinc enzyme is produced by pseudomonads, Flavobacterium sp. and Acinetobacter sp.
See also
- Glutamate carboxypeptidase II
References
- ^ Goldman, P. and Levy, C.C. (1967). "Carboxypeptidase G: purification and properties". Proc. Natl. Acad. Sci. USA 58: 1299–1306. PMID 5237864.
- ^ McCullogh, J.L., Chabner, B.A. and Bertino, J.R. (1971). "Purification and properties of carboxypeptidase G1". J. Biol. Chem. 246: 7207–7213. PMID 5129727.
- ^ Albrecht, A.M., Boldizar, E. and Hutchinson, D.J. (1978). "Carboxypeptidase displaying differential velocity in hydrolysis of methotrexate, 5-methyltetrahydrofolic acid, and leucovorin". J. Bacteriol. 134: 506–513. PMID 26657.
- ^ Sherwood, R.F., Melton, R.G. and Alwan, S.A. (1985). "Purification and properties of carboxypeptidase G2 from Pseudomonas sp. strain RS-16". Eur. J. Biochem. 148: 447–453. doi:10.1111/j.1432-1033.1985.tb08860.x. PMID 3838935.
External links
- Glutamate carboxypeptidase at the US National Library of Medicine Medical Subject Headings (MeSH)
|
Hydrolase: proteases (EC 3.4)
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|
| 3.4.11-19: Exopeptidase |
| 3.4.11 |
- Aminopeptidase
- Alanine
- Arginyl
- Aspartyl
- Cystinyl
- Leucyl
- Glutamyl
- Methionyl
- O
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| 3.4.13 |
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| 3.4.14 |
- Dipeptidyl peptidase
- Cathepsin C
- Dipeptidyl peptidase-4
- Tripeptidyl peptidase
- Tripeptidyl peptidase I
- Tripeptidyl peptidase II
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| 3.4.15 |
- Angiotensin-converting enzyme
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| 3.4.16 |
- Serine type carboxypeptidases: Cathepsin A
- DD-transpeptidase
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|
| 3.4.17 |
- Metalloexopeptidases
- Carboxypeptidase
- A
- A2
- B
- C
- E
- Glutamate II
|
|
| Other/ungrouped |
|
|
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| 3.4.21-25: Endopeptidase |
- Serine protease
- Cysteine protease
- Aspartic acid protease
- Metalloendopeptidase
- Threonine endopeptidase
- Proteasome endopeptidase complex
- HslU—HslV peptidase
- Other/ungrouped: Amyloid precursor protein secretase
- Alpha secretase
- Beta-secretase 1
- Beta-secretase 2
- Gamma secretase
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| 3.4.99: Unknown |
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Enzymes
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| Activity |
- Active site
- Binding site
- Catalytic triad
- Oxyanion hole
- Enzyme promiscuity
- Catalytically perfect enzyme
- Coenzyme
- Cofactor
- Enzyme catalysis
- Enzyme kinetics
- Lineweaver–Burk plot
- Michaelis–Menten kinetics
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| Regulation |
- Allosteric regulation
- Cooperativity
- Enzyme inhibitor
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| Classification |
- EC number
- Enzyme superfamily
- Enzyme family
- List of enzymes
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| Types |
- EC1 Oxidoreductases(list)
- EC2 Transferases(list)
- EC3 Hydrolases(list)
- EC4 Lyases(list)
- EC5 Isomerases(list)
- EC6 Ligases(list)
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UpToDate Contents
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English Journal
- Development and validation of a turbulent flow chromatography and tandem mass spectrometry method for the quantitation of methotrexate and its metabolites 7-hydroxy methotrexate and DAMPA in serum.
- Schofield RC1, Ramanathan LV1, Murata K1, Grace M2, Fleisher M1, Pessin MS1, Carlow DC3.
- Journal of chromatography. B, Analytical technologies in the biomedical and life sciences.J Chromatogr B Analyt Technol Biomed Life Sci.2015 Aug 22;1002:169-175. doi: 10.1016/j.jchromb.2015.08.025. [Epub ahead of print]
- A rapid and simple turbulent flow liquid chromatography (TFC-LC) method implementing positive heated electrospray ionization (HESI) for the accurate and precise determination of methotrexate (MTX), 7-hydroxy methotrexate (7-OH MTX), and 4-amino-4-deoxy-N10-methylpteroic acid (DAMPA) concentrations i
- PMID 26322588
- Putative bacterial volatile-mediated growth in soybean (Glycine max L. Merrill) and expression of induced proteins under salt stress.
- Vaishnav A1, Kumari S1, Jain S1, Varma A1, Choudhary DK1.
- Journal of applied microbiology.J Appl Microbiol.2015 Aug;119(2):539-51. doi: 10.1111/jam.12866. Epub 2015 Jun 25.
- AIMS: Plant root-associated rhizobacteria elicit plant immunity referred to as induced systemic tolerance (IST) against multiple abiotic stresses. Among multibacterial determinants involved in IST, the induction of IST and promotion of growth by putative bacterial volatile compounds (VOCs) is report
- PMID 26042866
Japanese Journal
- The complete nucleotide sequence of the Pseudomonas gene coding for carboxypeptidase G2.
Related Links
- Glucarpidase (Carboxypeptidase G2) Intervention in Adult and Elderly Cancer Patients with Renal Dysfunction and Delayed Methotrexate ... Stefan Schwartz a, Klaus Borner b, Krystina Müller a,
- Catalyzes the hydrolysis of reduced and non-reduced folates to pteroates and L-glutamate. This enzyme has a broad specificity. ... Release of C-terminal glutamate residues from a wide range of N-acylating moieties, including ...
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