Wikipedia preview
出典(authority):フリー百科事典『ウィキペディア(Wikipedia)』「2013/08/30 15:42:57」(JST)
[Wiki en表示]
In biochemistry, a hydrolase // is an enzyme that catalyzes the hydrolysis of a chemical bond. For example, an enzyme that catalyzed the following reaction is a hydrolase:
- A–B + H2O → A–OH + B–H
Contents
- 1 Nomenclature
- 2 Classification
- 3 References
- 4 See also
Nomenclature[edit source | edit]
Systematic names of hydrolases are formed as "substrate hydrolase." However, common names are typically in the form "substratease." For example, a nuclease is a hydrolase that cleaves nucleic acids.
Classification[edit source | edit]
Hydrolases are classified as EC 3 in the EC number classification of enzymes. Hydrolases can be further classified into several subclasses, based upon the bonds they act upon:
- EC 3.1: ester bonds (esterases: nucleases, phosphodiesterases, lipase, phosphatase)
- EC 3.2: sugars (DNA glycosylases, glycoside hydrolase)
- EC 3.3: ether bonds
- EC 3.4: peptide bonds (Proteases/peptidases)
- EC 3.5: carbon-nitrogen bonds, other than peptide bonds
- EC 3.6 acid anhydrides (acid anhydride hydrolases, including helicases and GTPase)
- EC 3.7 carbon-carbon bonds
- EC 3.8 halide bonds
- EC 3.9: phosphorus-nitrogen bonds
- EC 3.10: sulphur-nitrogen bonds
- EC 3.11: carbon-phosphorus bonds
- EC 3.12: sulfur-sulfur bonds
- EC 3.13: carbon-sulfur bonds
References[edit source | edit]
- EC 3 Introduction from the Department of Chemistry at Queen Mary, University of London, only covers 3.1-3.4
- More detailed taxonomy
See also[edit source | edit]
- Phosphorylase
- Serine hydrolase
Proteins: enzymes
|
|
Topics |
- Active site
- Allosteric regulation
- Binding site
- Catalytically perfect enzyme
- Coenzyme
- Cofactor
- Cooperativity
- EC number
- Enzyme catalysis
- Enzyme inhibitor
- Enzyme kinetics
- Lineweaver–Burk plot
- Michaelis–Menten kinetics
- Enzyme promiscuity
- List of enzymes
|
|
Types |
- EC1 Oxidoreductases/list
- EC2 Transferases/list
- EC3 Hydrolases/list
- EC4 Lyases/list
- EC5 Isomerases/list
- EC6 Ligases/list
|
|
- B
- enzm
- 1.1
- 2
- 3
- 4
- 5
- 6
- 7
- 8
- 10
- 11
- 13
- 14
- 15-18
- 2.1
- 3.1
- 4.1
- 5.1
- 6.1-3
|
|
|
|
Hydrolase: esterases (EC 3.1)
|
|
3.1.1: Carboxylic ester hydrolases |
- Cholinesterase
- Acetylcholinesterase
- Butyrylcholinesterase
- Pectinesterase
- 6-phosphogluconolactonase
- PAF acetylhydrolase
- Lipase
- Bile salt-dependent
- Gastric/Lingual
- Pancreatic
- Lysosomal
- Hormone-sensitive
- Endothelial
- Hepatic
- Lipoprotein
- Monoacylglycerol
- Diacylglycerol
|
|
3.1.2: Thioesterase |
- Palmitoyl protein thioesterase
- Ubiquitin carboxy-terminal hydrolase L1
|
|
3.1.3: Phosphatase |
- Alkaline phosphatase
- Acid phosphatase (Prostatic)/Tartrate-resistant acid phosphatase/Purple acid phosphatases
- Nucleotidase
- Glucose 6-phosphatase
- Fructose 1,6-bisphosphatase
- Phosphoprotein phosphatase
- OCRL
- Pyruvate dehydrogenase phosphatase
- Fructose 6-P,2-kinase:fructose 2,6-bisphosphatase
- PTEN
- Phytase
- Inositol-phosphate phosphatase
- Phosphoprotein phosphatase: Protein tyrosine phosphatase
- Protein serine/threonine phosphatase
- Dual-specificity phosphatase
|
|
3.1.4: Phosphodiesterase |
- Autotaxin
- Phospholipase
- Sphingomyelin phosphodiesterase
- PDE1
- PDE2
- PDE3
- PDE4A/PDE4B
- PDE5
- Lecithinase (Clostridium perfringens alpha toxin)
- Cyclic nucleotide phosphodiesterase
|
|
3.1.6: Sulfatase |
- arylsulfatase
- Arylsulfatase A
- Arylsulfatase B
- Arylsulfatase E
- Steroid sulfatase
- Galactosamine-6 sulfatase
- Iduronate-2-sulfatase
- N-acetylglucosamine-6-sulfatase
|
|
Nuclease (includes
deoxyribonuclease and
ribonuclease) |
3.1.11-16: Exonuclease |
Exodeoxyribonuclease |
|
|
Exoribonuclease |
|
|
|
3.1.21-31: Endonuclease |
Endodeoxyribonuclease |
- Deoxyribonuclease I
- Deoxyribonuclease II
- Deoxyribonuclease IV
- Restriction enzyme
- UvrABC endonuclease
|
|
Endoribonuclease |
- RNase III
- RNase H
- RNase P
- RNase A
- RNase T1
- RNA-induced silencing complex
|
|
either deoxy- or ribo- |
- Aspergillus nuclease S1
- Micrococcal nuclease
|
|
|
|
- B
- enzm
- 1.1
- 2
- 3
- 4
- 5
- 6
- 7
- 8
- 10
- 11
- 13
- 14
- 15-18
- 2.1
- 3.1
- 4.1
- 5.1
- 6.1-3
|
|
|
|
Hydrolase: sugar hydrolases (EC 3.2)
|
|
3.2.1: Glycoside hydrolases |
Disaccharidase |
- Sucrase/Sucrase-isomaltase/Invertase
- Maltase
- Trehalase
- Lactase
|
|
Glucosidases |
- Cellulase
- Alpha-glucosidase
- Acid
- Neutral AB
- Neutral C
- Beta-glucosidase
- Debranching enzyme
|
|
Other |
- Amylase
- Chitinase
- Lysozyme
- Neuraminidase
- NEU1
- NEU2
- NEU3
- NEU4
- Bacterial neuraminidase
- Viral neuraminidase
- Galactosidases
- alpha-Mannosidase
- Glucuronidase
- Hyaluronidase
- Pullulanase
- Glucosylceramidase
- Galactosylceramidase
- Alpha-N-acetylgalactosaminidase
- Alpha-N-acetylglucosaminidase
- Fucosidase
- Hexosaminidase
- Iduronidase
- Maltase-glucoamylase
- Heparanase
|
|
|
3.2.2: Hydrolysing
N-Glycosyl compounds |
- DNA glycosylases: Oxoguanine glycosylase
|
|
- B
- enzm
- 1.1
- 2
- 3
- 4
- 5
- 6
- 7
- 8
- 10
- 11
- 13
- 14
- 15-18
- 2.1
- 3.1
- 4.1
- 5.1
- 6.1-3
|
|
|
|
Hydrolases: ether bond (EC 3.3)
|
|
3.3.1 |
|
|
3.3.2 |
- Epoxide hydrolase
- Leukotriene-A4 hydrolase
|
|
- B
- enzm
- 1.1
- 2
- 3
- 4
- 5
- 6
- 7
- 8
- 10
- 11
- 13
- 14
- 15-18
- 2.1
- 3.1
- 4.1
- 5.1
- 6.1-3
|
|
|
|
Hydrolase: proteases (EC 3.4)
|
|
3.4.11-19: Exopeptidase |
3.4.11 |
- Aminopeptidase
- Alanine
- Arginyl
- Aspartyl
- Cystinyl
- Leucyl
- Glutamyl
- Methionyl
- O
|
|
3.4.13 |
|
|
3.4.14 |
- Dipeptidyl peptidase
- Cathepsin C
- Dipeptidyl peptidase-4
- Tripeptidyl peptidase
- Tripeptidyl peptidase I
- Tripeptidyl peptidase II
|
|
3.4.15 |
- Angiotensin-converting enzyme
|
|
3.4.16 |
- Serine type carboxypeptidases: Cathepsin A
- DD-transpeptidase
|
|
3.4.17 |
- Metallocarboxypeptidases: Carboxypeptidase
|
|
Other/ungrouped |
|
|
|
3.4.21-24: Endopeptidase |
- Serine proteases
- Cysteine protease
- Aspartic acid protease
- Metalloendopeptidases
- Other/ungrouped: Amyloid precursor protein secretase
- Alpha secretase
- Beta-secretase 1
- Beta-secretase 2
- Gamma secretase
|
|
3.4.99: Unknown |
|
|
- B
- enzm
- 1.1
- 2
- 3
- 4
- 5
- 6
- 7
- 8
- 10
- 11
- 13
- 14
- 15-18
- 2.1
- 3.1
- 4.1
- 5.1
- 6.1-3
|
|
|
|
Hydrolases: carbon-nitrogen non-peptide (EC 3.5)
|
|
3.5.1: Linear amides /
Amidohydrolases |
- Asparaginase
- Glutaminase
- Urease
- Biotinidase
- Aspartoacylase
- Ceramidase
- Aspartylglucosaminidase
- Fatty acid amide hydrolase
- Histone deacetylase
|
|
3.5.2: Cyclic amides/
Amidohydrolases |
- Barbiturase
- Beta-lactamase
|
|
3.5.3: Linear amidines/
Ureohydrolases |
- Arginase
- Agmatinase
- Protein-arginine deiminase
|
|
3.5.4: Cyclic amidines/
Aminohydrolases |
- Guanine deaminase
- Adenosine deaminase
- AMP deaminase
- Inosine monophosphate synthase
- DCMP deaminase
- GTP cyclohydrolase I
- Cytidine deaminase
- AICDA
- Activation-Induced (Cytidine) Deaminase
|
|
3.5.5: Nitriles/
Aminohydrolases |
|
|
3.5.99: Other |
- Riboflavinase
- Thiaminase II
|
|
- B
- enzm
- 1.1
- 2
- 3
- 4
- 5
- 6
- 7
- 8
- 10
- 11
- 13
- 14
- 15-18
- 2.1
- 3.1
- 4.1
- 5.1
- 6.1-3
|
|
|
|
Hydrolases: acid anhydride hydrolases (EC 3.6)
|
|
3.6.1 |
- Pyrophosphatase
- Apyrase
- Thiamine-triphosphatase
|
|
3.6.2 |
- Adenylylsulfatase
- Phosphoadenylylsulfatase
|
|
3.6.3-4: ATPase |
3.6.3 |
Cu++ (3.6.3.4) |
- Menkes/ATP7A
- Wilson/ATP7B
|
|
Ca+ (3.6.3.8) |
- SERCA
- Plasma membrane
- ATP2B1
- ATP2B2
- ATP2B3
- ATP2B4
- SPCA
|
|
Na+/K+ (3.6.3.9) |
- ATP1A1
- ATP1A2
- ATP1A3
- ATP1A4
- ATP1B1
- ATP1B2
- ATP1B3
- ATP1B4
|
|
H+/K+ (3.6.3.10) |
|
|
Other P-type ATPase |
- ATP8B1
- ATP10A
- ATP11B
- ATP12A
- ATP13A2
- ATP13A3
|
|
|
3.6.4 |
- Dynein
- Kinesin
- Myosin
- Katanin
|
|
|
3.6.5: GTPase |
3.6.5.1: Heterotrimeric G protein |
- Gαs
- Gαi
- Gαq/11
- Gα12/13
- Transducin
|
|
3.6.5.2: Small GTPase > Ras superfamily |
- Rho family of GTPases: Cdc42
- RhoUV
- Rac
- RhoBTB
- RhoH
- Rho
- Rnd
- RhoDF
- other: Ras
- Rab
- Arf
- Ran
- Rheb
- Rap
- RGK
|
|
3.6.5.3: Protein-synthesizing GTPase |
|
|
3.6.5.5-6: Polymerization motors |
|
|
|
- B
- enzm
- 1.1
- 2
- 3
- 4
- 5
- 6
- 7
- 8
- 10
- 11
- 13
- 14
- 15-18
- 2.1
- 3.1
- 4.1
- 5.1
- 6.1-3
|
|
|
|
Hydrolases: carbon-carbon (EC 3.7)
|
|
3.7.1 |
- Fumarylacetoacetate hydrolase
- Kynureninase
|
|
- B
- enzm
- 1.1
- 2
- 3
- 4
- 5
- 6
- 7
- 8
- 10
- 11
- 13
- 14
- 15-18
- 2.1
- 3.1
- 4.1
- 5.1
- 6.1-3
|
|
|
|
UpToDate Contents
全文を閲覧するには購読必要です。 To read the full text you will need to subscribe.
English Journal
- The roles of the zinc finger transcription factors XlnR, ClrA and ClrB in the breakdown of lignocellulose by Aspergillus niger.
- Raulo R1, Kokolski M2, Archer DB3.
- AMB Express.AMB Express.2016 Dec;6(1):5. doi: 10.1186/s13568-016-0177-0. Epub 2016 Jan 16.
- Genes encoding the key transcription factors (TF) XlnR, ClrA and ClrB were deleted from Aspergillus niger and the resulting strains were assessed for growth on glucose and wheat straw, transcription of genes encoding glycosyl hydrolases and saccharification activity. Growth of all mutant strains, ba
- PMID 26780227
- Penicillin acylases revisited: importance beyond their industrial utility.
- Avinash VS1, Pundle AV1, Ramasamy S1, Suresh CG1.
- Critical reviews in biotechnology.Crit Rev Biotechnol.2016 Apr;36(2):303-16. doi: 10.3109/07388551.2014.960359. Epub 2014 Nov 28.
- It is of great importance to study the physiological roles of enzymes in nature; however, in some cases, it is not easily apparent. Penicillin acylases are pharmaceutically important enzymes that cleave the acyl side chains of penicillins, thus paving the way for production of newer semi-synthetic a
- PMID 25430891
- High-resolution proteomic profiling of spider venom: expanding the toxin diversity of Phoneutria nigriventer venom.
- Liberato T1,2, Troncone LR1, Yamashiro ET3, Serrano SM3, Zelanis A4,5.
- Amino acids.Amino Acids.2016 Mar;48(3):901-6. doi: 10.1007/s00726-015-2151-6. Epub 2016 Jan 23.
- Here we present a proteomic characterization of Phoneutria nigriventer venom. A shotgun proteomic approach allowed the identification, for the first time, of O-glycosyl hydrolases (chitinases) in P. nigriventer venom. The electrophoretic profiles under nonreducing and reducing conditions, and protei
- PMID 26803659
Japanese Journal
- 糖質加水分解酵素の潜在的機能を活用した特殊オリゴ糖の合成
- Expression of key hydrolases for soy sauce fermentation in Zygosaccharomyces rouxii
- Yuzuki Masanobu,Matsushima Kenichiro,Koyama Yasuji
- Journal of bioscience and bioengineering 119(1), 92-94, 2015-01
- NAID 40020349972
- Expression of key hydrolases for soy sauce fermentation in Zygosaccharomyces rouxii(BREWING AND FOOD TECHNOLOGY)
- Yuzuki Masanobu,Matsushima Kenichiro,Koyama Yasuji
- Journal of bioscience and bioengineering 119(1), 92-94, 2015-01
- … Several key hydrolases in soy sauce fermentation such as proteases, peptidases, and glutaminases are supplied by Aspergillus sojae or Aspergillus oryzae. … The genes encoding these hydrolases were successfully expressed in salt-tolerant yeast Zygosaccharomyces rouxii. … These transformants are expected to supply extra hydrolases during soy sauce fermentation process. …
- NAID 110009892240
Related Links
- Objective: Knowing that the lysosomes contain a powerful cocktail of hydrolases capable of digesting cells and entire tissues, it is obvious that the maintenance of lysosomal membrane integrity is of utmost importance for all cells ...
- Hydrolases a class of enzymes that catalyze reactions of hydrolytic decomposition (with the participation of water) of intramolecular bonds (hydrolysis). Hydrolases are widespread in plant and animal cells. They participate in ...
Related Pictures
★リンクテーブル★
[★]
エポキシドヒドロラーゼ
[★]