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出典(authority):フリー百科事典『ウィキペディア(Wikipedia)』「2016/01/24 12:00:50」(JST)
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Phosphorylase |
Identifiers |
EC number |
2.4.1.1 |
CAS number |
9035-74-9 |
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 |
|
Phosphorylases are enzymes that catalyze the addition of a phosphate group from an inorganic phosphate (phosphate+hydrogen) to an acceptor.
- A-B + P A + P-B
They include allosteric enzymes that catalyze the production of glucose-1-phosphate from a glucan such as glycogen, starch or maltodextrin. Phosphorylase is also a common name used for glycogen phosphorylase in honor of Earl W. Sutherland Jr. who in the late 1930s discovered the first phosphorylase.[1]
Contents
- 1 Function
- 2 Types
- 3 Activation
- 4 Pathology
- 5 See also
- 6 References
- 7 External links
FunctionEdit
Phosphorylases should not be confused with phosphatases, which remove phosphate groups. In more general terms, phosphorylases are enzymes that catalyze the addition of a phosphate group from an inorganic phosphate (phosphate + hydrogen) to an acceptor, not to be confused with a phosphatase (a hydrolase) or a kinase (a phosphotransferase). A phosphatase removes a phosphonate group from a donor using water, whereas a kinase transfers a phosphonate group from a donor (usually ATP) to an acceptor.
Enzyme name |
Enzymes class |
Reaction |
Notes |
Phosphorylase |
Transferase
(EC 2.4 and EC 2.7.7) |
A-B + H-OP A-OP + H-B |
transfer group = A = glycosyl- group or
nucleotidyl- group |
Phosphatase |
Hydrolase
(EC 3) |
P-B + H-OH P-OH + H-B |
|
Kinase |
Transferase
(EC 2.7.1-2.7.4) |
P-B + H-A P-A + H-B |
transfer group = P |
P = phosphonate group, OP = phosphate group, H-OP or P-OH = inorganic phosphate |
TypesEdit
The phosphorylases fall into the following categories:
- Glycosyltransferases (EC 2.4)
- Enzymes that break down glucans by removing a glucose residue (break O-glycosidic bond)
- glycogen phosphorylase
- starch phosphorylase
- maltodextrin phosphorylase
- Enzymes that break down nucleosides into their constituent bases and sugars (break N-glycosidic bond)
- Purine nucleoside phosphorylase (PNPase)
- Nucleotidyltransferases (EC 2.7.7)
- Enzymes that have phosphorolytic 3' to 5' exoribonuclease activity (break phosphodiester bond)
- RNase PH
- Polynucleotide Phosphorylase (PNPase)
All known phosphorylases share catalytic and structural properties [1].
ActivationEdit
Phosphorylase a is the active form of glycogen phosphorylase that is derived from the phosphorylation of the inactive form, phosphorylase b.
PathologyEdit
Some disorders are related to phosphorylases:
- Glycogen storage disease type V - muscle glycogen
- Glycogen storage disease type VI - liver glycogen
See alsoEdit
ReferencesEdit
- ^ Lehninger Principles of Biochemistry 5th ed. pg. 603
External linksEdit
- Muscle phosphorylase deficiency - McArdle's Disease Website
- Phosphorylases at the US National Library of Medicine Medical Subject Headings (MeSH)
Transferases: phosphorus-containing groups (EC 2.7)
|
|
2.7.1-2.7.4:
phosphotransferase/kinase
(PO4) |
2.7.1: OH acceptor |
- Hexo-
- Gluco-
- Fructo-
- Galacto-
- Phosphofructo-
- 1
- Liver
- Muscle
- Platelet
- 2
- Riboflavin
- Shikimate
- Thymidine
- NAD+
- Glycerol
- Pantothenate
- Mevalonate
- Pyruvate
- Deoxycytidine
- PFP
- Diacylglycerol
- Phosphoinositide 3
- Class I PI 3
- Class II PI 3
- Sphingosine
- Glucose-1,6-bisphosphate synthase
|
|
2.7.2: COOH acceptor |
- Phosphoglycerate
- Aspartate kinase
|
|
2.7.3: N acceptor |
|
|
2.7.4: PO4 acceptor |
- Phosphomevalonate
- Adenylate
- Nucleoside-diphosphate
- Uridylate
- Guanylate
- Thiamine-diphosphate
|
|
|
2.7.6: diphosphotransferase
(P2O7) |
- Ribose-phosphate diphosphokinase
- Thiamine diphosphokinase
|
|
2.7.7: nucleotidyltransferase
(PO4-nucleoside) |
Polymerase |
DNA polymerase |
- DNA-directed DNA polymerase
- I
- II
- III
- IV
- V
- RNA-directed DNA polymerase
- Reverse transcriptase
- Telomerase
- DNA nucleotidylexotransferase/Terminal deoxynucleotidyl transferase
|
|
RNA nucleotidyltransferase |
- RNA polymerase/DNA-directed RNA polymerase
- RNA polymerase I
- RNA polymerase II
- RNA polymerase III
- RNA polymerase IV
- Primase
- RNA-dependent RNA polymerase
- PNPase
|
|
|
Phosphorolytic
3' to 5' exoribonuclease |
|
|
Nucleotidyltransferase |
- UTP—glucose-1-phosphate uridylyltransferase
- Galactose-1-phosphate uridylyltransferase
|
|
Guanylyltransferase |
|
|
Other |
- Recombinase (Integrase)
- Transposase
|
|
|
2.7.8: miscellaneous |
Phosphatidyltransferases |
- CDP-diacylglycerol—glycerol-3-phosphate 3-phosphatidyltransferase
- CDP-diacylglycerol—serine O-phosphatidyltransferase
- CDP-diacylglycerol—inositol 3-phosphatidyltransferase
- CDP-diacylglycerol—choline O-phosphatidyltransferase
|
|
Glycosyl-1-phosphotransferase |
- N-acetylglucosamine-1-phosphate transferase
|
|
|
2.7.10-2.7.13: protein kinase
(PO4; protein acceptor) |
2.7.10: protein-tyrosine |
|
|
2.7.11: protein-serine/threonine |
- see serine/threonine-specific protein kinases
|
|
2.7.12: protein-dual-specificity |
- see serine/threonine-specific protein kinases
|
|
2.7.13: protein-histidine |
- Protein-histidine pros-kinase
- Protein-histidine tele-kinase
- Histidine kinase
|
|
|
- Biochemistry overview
- Enzymes overview
- By EC number: 1.1
- 2
- 3
- 4
- 5
- 6
- 7
- 8
- 9
- 10
- 11
- 12
- 13
- 14
- 15-99
- 2.1
- 3.1
- 4.1
- 5.1
- 6.1-3
|
|
|
|
Transferases: glycosyltransferases (EC 2.4)
|
|
2.4.1: Hexosyl-
transferases |
Glucosyl- |
- Phosphorylase
- Glycogen synthase
- Debranching enzyme
- Branching enzyme
- 1,3-Beta-glucan synthase
- Ceramide glucosyltransferase
|
|
Galactosyl- |
- Lactose synthase
- B-N-acetylglucosaminyl-glycopeptide b-1,4-galactosyltransferase
- Glycoprotein-N-acetylgalactosamine 3-beta-galactosyltransferase (C1GALT1)
|
|
Glucuronosyl- |
- UGT1A1
- UGT1A3
- UGT1A4
- UGT1A5
- UGT1A6
- UGT1A7
- UGT1A8
- UGT1A9
- UGT1A10
- UGT2A1
- UGT2A2
- UGT2A3
- UGT2B4
- UGT2B7
- UGT2B10
- UGT2B11
- UGT2B15
- UGT2B17
- UGT2B28
- Hyaluronan synthase: HAS1
- HAS2
- HAS3
|
|
Fucosyl- |
- POFUT1
- POFUT2
- FUT1
- FUT2
- FUT3
- FUT4
- FUT5
- FUT6
- FUT7
- FUT8
- FUT9
- FUT10
- FUT11
|
|
Mannosyl- |
- Dolichyl-phosphate-mannose-protein mannosyltransferase
- DPM1
- DPM3
- ALG1
- ALG2
- ALG3
- ALG6
- ALG8
- ALG9
- ALG12
|
|
|
2.4.2: Pentosyl-
transferases |
Ribose |
ADP-ribosyltransferase |
- NAD+:diphthamide ADP-ribosyltransferase
- NAD(P)+:arginine ADP-ribosyltransferase
- Pertussis toxin
- Cholera toxin
- Poly ADP ribose polymerase
|
|
Phosphoribosyltransferase |
- Adenine phosphoribosyltransferase
- Hypoxanthine-guanine phosphoribosyltransferase
- Uracil phosphoribosyltransferase
- Amidophosphoribosyltransferase
|
|
Other |
- Purine nucleoside phosphorylase: Thymidine phosphorylase
|
|
|
Other |
- Xylosyltransferase
- Arabinosyltransferase
- Indolylacetylinositol arabinosyltransferase
|
|
|
2.4.99: Sialyl
transferases |
- Beta-galactoside alpha-2,6-sialyltransferase
- Monosialoganglioside sialyltransferase
- ST8SIA4
|
|
- Biochemistry overview
- Enzymes overview
- By EC number: 1.1
- 2
- 3
- 4
- 5
- 6
- 7
- 8
- 9
- 10
- 11
- 12
- 13
- 14
- 15-99
- 2.1
- 3.1
- 4.1
- 5.1
- 6.1-3
|
|
|
|
Proteins: enzymes
|
|
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
|
|
Regulation |
- Allosteric regulation
- Cooperativity
- Enzyme inhibitor
|
|
Classification |
- EC number
- Enzyme superfamily
- Enzyme family
- List of enzymes
|
|
Types |
- EC1 Oxidoreductases(list)
- EC2 Transferases(list)
- EC3 Hydrolases(list)
- EC4 Lyases(list)
- EC5 Isomerases(list)
- EC6 Ligases(list)
|
|
- Biochemistry overview
- Enzymes overview
- By EC number: 1.1
- 2
- 3
- 4
- 5
- 6
- 7
- 8
- 9
- 10
- 11
- 12
- 13
- 14
- 15-99
- 2.1
- 3.1
- 4.1
- 5.1
- 6.1-3
|
|
|
|
UpToDate Contents
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English Journal
- Properties of a glycogen like polysaccharide produced by a mutant of Escherichia coli lacking glycogen synthase and maltodextrin phosphorylase.
- Kwak JY1, Kim MG2, Kim YW2, Ban HS3, Won MS3, Park JT4, Park KH5.
- Carbohydrate polymers.Carbohydr Polym.2016 Jan 20;136:649-55. doi: 10.1016/j.carbpol.2015.09.091. Epub 2015 Sep 30.
- Escherichia coli mutant TBP38 lacks glycogen synthase (GlgA) and maltodextrin phosphorylase (MalP). When grown on maltose in fed-batch fermentation TBP38 accumulated more than 50-fold higher glycogen-type polysaccharide than its parental strain. The polysaccharides were extracted at different growth
- PMID 26572397
- Urine Purine Metabolite Determination by UPLC-Tandem Mass Spectrometry.
- Sun Q1.
- Methods in molecular biology (Clifton, N.J.).Methods Mol Biol.2016;1378:227-35. doi: 10.1007/978-1-4939-3182-8_24.
- Inborn errors of purine metabolism, either deficiencies of synthesis or catabolism pathways, lead to a wide spectrum of clinical presentations: urolithiasis (adenine phosphoribosyltransferase), primary immune deficiency (adenosine deaminase deficiency and purine nucleoside phosphorylase deficiency),
- PMID 26602134
- CsrA Participates in a PNPase Autoregulatory Mechanism by Selectively Repressing Translation of pnp Transcripts That Have Been Previously Processed by RNase III and PNPase.
- Park H1, Yakhnin H1, Connolly M1, Romeo T2, Babitzke P3.
- Journal of bacteriology.J Bacteriol.2015 Dec 15;197(24):3751-9. doi: 10.1128/JB.00721-15. Epub 2015 Oct 5.
- Csr is a conserved global regulatory system that represses or activates gene expression posttranscriptionally. CsrA of Escherichia coli is a homodimeric RNA binding protein that regulates transcription elongation, translation initiation, and mRNA stability by binding to the 5' untranslated leader or
- PMID 26438818
Japanese Journal
- Production and application of a rare disaccharide using sucrose phosphorylase from Leuconostoc mesenteroides
- Morimoto Kenji,Yoshihara Akihide,Furumoto Toshio [他]
- Journal of bioscience and bioengineering 119(6), 652-656, 2015-06
- NAID 40020500246
- Properties and functions of the storage sites of glycogen phosphorylase
- Makino Yasushi,Fujii Yuta,Taniguchi Motoi
- The journal of biochemistry 157(6), 451-458, 2015-06
- NAID 40020489240
- Ochromonas danica由来1,3-β-グルカンホスホリラーゼの特性と応用(応用糖質科学シンポジウム)
- 磯野 直人,山本 豊,西尾 昌洋,梅川 逸人,久松 眞
- 応用糖質科学 : 日本応用糖質科学会誌 5(2), 128-134, 2015-05-20
- 1,3-β-グルカンホスホリラーゼ(BGP)は1,3-β-グルコシド結合の加リン酸分解を可逆的に触媒する酵素である。BGPは40年以上前に発見された酵素であるが,研究報告がほとんどなく,詳細な性質が明らかにされてこなかった。本研究ではOchromonas danica由来BGP(OdBGP)の特性と一次構造を調べた。本酵素は三糖以上のラミナリオリゴ糖からラミナリンまで,幅広い分子量の糖質の加リン酸 …
- NAID 110009964190
Related Links
- ホスホリラーゼ【phosphorylase】とは。意味や解説、類語。でんぷん・グリコーゲンなどを加燐酸(かりんさん)分解する酵素の総称。フォスフォリラーゼ。ホスホリラーゼホスファターゼ【phosphorylase phosphatase】⇒プロテインホスファターゼ
- phosphorylase /phos·phor·y·lase/ (fos-for´ĭ-lās) 1. any of a group of enzymes that catalyze the phosphorolysis of glycosides, transferring the cleaved glycosyl group to inorganic phosphate. When not qualified with the substrate name ...
Related Pictures
★リンクテーブル★
[★]
- 英
- phosphorylase, PR
- 同
- リン酸付加分解酵素、グリコーゲンホスホリラーゼ glycogen phosphorylase、アミロホスホリラーゼ amylophosphorylase
[★]
[★]
- 英
- pyrophosphorylase
- 関
- ホスホリラーゼ phosphorylase
[★]
- 英
- phosphorylase
- 関
- ホスホリラーゼ
[★]
- 同
- PNP deficiency
- 同
- PNP deficiency
[★]
UDPグルコースピロホスホリラーゼ
[★]
UDPグルコースピロホスホリラーゼ
[★]
肝ホスホリラーゼ欠損性糖原病
[★]
ウリジンホスホリラーゼ