Phosphorylase

Class of enzymes
Phosphorylase
Identifiers
EC no.2.4.1.1
CAS no.9035-74-9
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In biochemistry, 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 it as the first phosphorylase.[1]

Function

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 phosphate group from a donor using water, whereas a kinase transfers a phosphate 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

Types

The phosphorylases fall into the following categories:

All known phosphorylases share catalytic and structural properties.[2]

Activation

Phosphorylase a is the more active R form of glycogen phosphorylase that is derived from the phosphorylation of the less active R form, phosphorylase b with associated AMP. The inactive T form is either phosphorylated by phosphoylase kinase and inhibited by glucose, or dephosphorylated by phosphoprotein phosphatase with inhibition by ATP and/or glucose 6-phosphate. Phosphorylation requires ATP but dephosphorylation releases free inorganic phosphate ions.

Pathology

Some disorders are related to phosphorylases:

See also

References

  1. ^ Nelson DL, Lehninger AL, Cox MM (2005). Lehninger Principles of Biochemistry (5th ed.). W. H. Freeman. p. 603. ISBN 978-0-7167-4339-2.
  2. ^ "PROSITE documentation PDOC00095 [for PROSITE entry PS00102]". PROSITE.

External links

  • Muscle phosphorylase deficiency - McArdle's Disease Website
  • Phosphorylases at the U.S. National Library of Medicine Medical Subject Headings (MeSH)
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Transferases: phosphorus-containing groups (EC 2.7)
2.7.1-2.7.4:
phosphotransferase/kinase
(PO4)
2.7.1: OH acceptor
2.7.2: COOH acceptor
2.7.3: N acceptor
2.7.4: PO4 acceptor
2.7.6: diphosphotransferase
(P2O7)2.7.7: nucleotidyltransferase
(PO4-nucleoside)
Polymerase
DNA polymerase
DNA-directed DNA polymerase
I/A
γ
θ
ν
T7
Taq
II/B
α
δ
ε
ζ
Pfu
III/C
IV/X
β
λ
μ
TDT
V/Y
η
ι
κ
RNA-directed DNA polymerase
Reverse transcriptase
Telomerase
RNA polymerase
Phosphorolytic
3' to 5' exoribonuclease
Nucleotidyltransferase
Guanylyltransferase
Other
2.7.8: miscellaneous
Phosphatidyltransferases
Glycosyl-1-phosphotransferase
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
  • v
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2.4.1: Hexosyl-
transferases
Glucosyl-
Galactosyl-
Glucuronosyl-
Fucosyl-
Mannosyl-
2.4.2: Pentosyl-
transferases
Ribose
ADP-ribosyltransferase
Phosphoribosyltransferase
Other
Other
2.4.99: Sialyl
transferases
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