Specificity determinants for the AMP-activated protein kinase and its plant homologue analysed using synthetic peptides

J Weekes; K L Ball; F B Caudwell; D G Hardie

doi:10.1016/0014-5793(93)80706-Z

Specificity determinants for the AMP-activated protein kinase and its plant homologue analysed using synthetic peptides

J Weekes, K L Ball, F B Caudwell, D G Hardie

Research output: Contribution to journal › Article › peer-review

Abstract / Description of output

Inspection of sequences around sites phosphorylated by the AMP-activated protein kinase (AMP-PK), and homologous sequences from other species, indicates conserved features. There are hydrophobic residues (M, V, L, I) at P-5 and P+4, and at least one basic residue (R, K, H) at P-2, P-3 or P-4. The importance of these residues has been established for AMP-PK and its putative plant homologue using a series of synthetic peptides. These results confirm the functional similarity of the animal and plant kinases, and suggest that the required motif for recognition of substrate by either kinase is M/V/L/I-(R/K/H,X,X)-X-S/T-X-X-X-M/V/L/I.

Original language	English
Pages (from-to)	335-9
Number of pages	5
Journal	FEBS Letters
Volume	334
Issue number	3
DOIs	https://doi.org/10.1016/0014-5793(93)80706-Z
Publication status	Published - 22 Nov 1993

Keywords / Materials (for Non-textual outputs)

AMP-Activated Protein Kinases
Acetyl-CoA Carboxylase
Amino Acid Sequence
Animals
Glycogen Synthase
Humans
Liver
Molecular Sequence Data
Multienzyme Complexes
Peptides
Plants
Protein Kinases
Protein-Serine-Threonine Kinases
Rats
Sequence Homology, Amino Acid
Substrate Specificity

Access to Document

10.1016/0014-5793(93)80706-Z

Specificity determinants for the AMP-activated protein kinase
FEBS Letters open archive
Final published version, 528 KB

http://www.sciencedirect.com/science/article/pii/001457939380706Z

Cite this

@article{7367999e62c54b2383853ac2864877df,

title = "Specificity determinants for the AMP-activated protein kinase and its plant homologue analysed using synthetic peptides",

abstract = "Inspection of sequences around sites phosphorylated by the AMP-activated protein kinase (AMP-PK), and homologous sequences from other species, indicates conserved features. There are hydrophobic residues (M, V, L, I) at P-5 and P+4, and at least one basic residue (R, K, H) at P-2, P-3 or P-4. The importance of these residues has been established for AMP-PK and its putative plant homologue using a series of synthetic peptides. These results confirm the functional similarity of the animal and plant kinases, and suggest that the required motif for recognition of substrate by either kinase is M/V/L/I-(R/K/H,X,X)-X-S/T-X-X-X-M/V/L/I.",

keywords = "AMP-Activated Protein Kinases, Acetyl-CoA Carboxylase, Amino Acid Sequence, Animals, Glycogen Synthase, Humans, Liver, Molecular Sequence Data, Multienzyme Complexes, Peptides, Plants, Protein Kinases, Protein-Serine-Threonine Kinases, Rats, Sequence Homology, Amino Acid, Substrate Specificity",

author = "J Weekes and Ball, {K L} and Caudwell, {F B} and Hardie, {D G}",

year = "1993",

month = nov,

day = "22",

doi = "10.1016/0014-5793(93)80706-Z",

language = "English",

volume = "334",

pages = "335--9",

journal = "FEBS Letters",

issn = "0014-5793",

publisher = "Elsevier",

number = "3",

}

TY - JOUR

T1 - Specificity determinants for the AMP-activated protein kinase and its plant homologue analysed using synthetic peptides

AU - Weekes, J

AU - Ball, K L

AU - Caudwell, F B

AU - Hardie, D G

PY - 1993/11/22

Y1 - 1993/11/22

N2 - Inspection of sequences around sites phosphorylated by the AMP-activated protein kinase (AMP-PK), and homologous sequences from other species, indicates conserved features. There are hydrophobic residues (M, V, L, I) at P-5 and P+4, and at least one basic residue (R, K, H) at P-2, P-3 or P-4. The importance of these residues has been established for AMP-PK and its putative plant homologue using a series of synthetic peptides. These results confirm the functional similarity of the animal and plant kinases, and suggest that the required motif for recognition of substrate by either kinase is M/V/L/I-(R/K/H,X,X)-X-S/T-X-X-X-M/V/L/I.

AB - Inspection of sequences around sites phosphorylated by the AMP-activated protein kinase (AMP-PK), and homologous sequences from other species, indicates conserved features. There are hydrophobic residues (M, V, L, I) at P-5 and P+4, and at least one basic residue (R, K, H) at P-2, P-3 or P-4. The importance of these residues has been established for AMP-PK and its putative plant homologue using a series of synthetic peptides. These results confirm the functional similarity of the animal and plant kinases, and suggest that the required motif for recognition of substrate by either kinase is M/V/L/I-(R/K/H,X,X)-X-S/T-X-X-X-M/V/L/I.

KW - AMP-Activated Protein Kinases

KW - Acetyl-CoA Carboxylase

KW - Amino Acid Sequence

KW - Animals

KW - Glycogen Synthase

KW - Humans

KW - Liver

KW - Molecular Sequence Data

KW - Multienzyme Complexes

KW - Peptides

KW - Plants

KW - Protein Kinases

KW - Protein-Serine-Threonine Kinases

KW - Rats

KW - Sequence Homology, Amino Acid

KW - Substrate Specificity

U2 - 10.1016/0014-5793(93)80706-Z

DO - 10.1016/0014-5793(93)80706-Z

M3 - Article

C2 - 7902296

SN - 0014-5793

VL - 334

SP - 335

EP - 339

JO - FEBS Letters

JF - FEBS Letters

IS - 3

ER -

Specificity determinants for the AMP-activated protein kinase and its plant homologue analysed using synthetic peptides

Abstract / Description of output

Keywords / Materials (for Non-textual outputs)

Access to Document

Fingerprint

Cite this