L-threonine kinase

Last updated
L-threonine kinase
Identifiers
EC no. 2.7.1.177
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

L-threonine kinase (EC 2.7.1.177, PduX) is an enzyme with systematic name ATP:L-threonine O3-phosphotransferase. [1] [2] This enzyme catalyses the following chemical reaction

ATP + L-threonine ADP + O-phospho-L-threonine

The enzyme takes part in the synthesis of adenosylcobalamin.

Related Research Articles

<span class="mw-page-title-main">Caveolin 1</span> Protein-coding gene in the species Homo sapiens

Caveolin-1 is a protein that in humans is encoded by the CAV1 gene.

<span class="mw-page-title-main">PRKCB1</span> Protein-coding gene in the species Homo sapiens

Protein kinase C beta type is an enzyme that in humans is encoded by the PRKCB gene.

<span class="mw-page-title-main">DAPK1</span> Protein-coding gene in the species Homo sapiens

Death-associated protein kinase 1 is an enzyme that in humans is encoded by the DAPK1 gene.

<span class="mw-page-title-main">RPS6KA1</span> Enzyme

Ribosomal protein S6 kinase alpha-1 is an enzyme that in humans is encoded by the RPS6KA1 gene.

<span class="mw-page-title-main">IRAK1</span> Protein-coding gene in the species Homo sapiens

Interleukin-1 receptor-associated kinase 1 (IRAK-1) is an enzyme in humans encoded by the IRAK1 gene. IRAK-1 plays an important role in the regulation of the expression of inflammatory genes by immune cells, such as monocytes and macrophages, which in turn help the immune system in eliminating bacteria, viruses, and other pathogens. IRAK-1 is part of the IRAK family consisting of IRAK-1, IRAK-2, IRAK-3, and IRAK-4, and is activated by inflammatory molecules released by signaling pathways during pathogenic attack. IRAK-1 is classified as a kinase enzyme, which regulates pathways in both innate and adaptive immune systems.

In enzymology, an elongation factor 2 kinase is an enzyme that catalyzes the chemical reaction:

In enzymology, a [isocitrate dehydrogenase (NADP+)] kinase (EC 2.7.11.5) is an enzyme that catalyzes the chemical reaction:

<span class="mw-page-title-main">P70-S6 Kinase 1</span> Protein-coding gene in the species Homo sapiens

Ribosomal protein S6 kinase beta-1 (S6K1), also known as p70S6 kinase, is an enzyme that in humans is encoded by the RPS6KB1 gene. It is a serine/threonine kinase that acts downstream of PIP3 and phosphoinositide-dependent kinase-1 in the PI3 kinase pathway. As the name suggests, its target substrate is the S6 ribosomal protein. Phosphorylation of S6 induces protein synthesis at the ribosome.

<span class="mw-page-title-main">Protein kinase, AMP-activated, alpha 1</span> Protein-coding gene in the species Homo sapiens

5'-AMP-activated protein kinase catalytic subunit alpha-1 is an enzyme that in humans is encoded by the PRKAA1 gene.

<span class="mw-page-title-main">MAP2K7</span> Protein-coding gene in the species Homo sapiens

Dual specificity mitogen-activated protein kinase kinase 7, also known as MAP kinase kinase 7 or MKK7, is an enzyme that in humans is encoded by the MAP2K7 gene. This protein is a member of the mitogen-activated protein kinase kinase family. The MKK7 protein exists as six different isoforms with three possible N-termini and two possible C-termini.

<span class="mw-page-title-main">PDK2</span> Protein-coding gene in the species Homo sapiens

Pyruvate dehydrogenase kinase isoform 2 (PDK2) also known as pyruvate dehydrogenase lipoamide kinase isozyme 2, mitochondrial is an enzyme that in humans is encoded by the PDK2 gene. PDK2 is an isozyme of pyruvate dehydrogenase kinase.

<span class="mw-page-title-main">PIKFYVE</span> Protein-coding gene in the species Homo sapiens

PIKfyve, a FYVE finger-containing phosphoinositide kinase, is an enzyme that in humans is encoded by the PIKFYVE gene.

<span class="mw-page-title-main">RIPK3</span> Protein-coding gene in humans

Receptor-interacting serine/threonine-protein kinase 3 is an enzyme that is encoded by the RIPK3 gene in humans.

<span class="mw-page-title-main">DUSP4</span> Protein-coding gene in the species Homo sapiens

Dual specificity protein phosphatase 4 is an enzyme that in humans is encoded by the DUSP4 gene.

<span class="mw-page-title-main">IRAK2</span> Protein-coding gene in the species Homo sapiens

Interleukin-1 receptor-associated kinase-like 2 is an enzyme that in humans is encoded by the IRAK2 gene.

<span class="mw-page-title-main">Bacterial microcompartment</span> Organelle-like structure in bacteria with a protein shell containing enzymes

Bacterial microcompartments (BMCs) are organelle-like structures found in bacteria. They consist of a protein shell that encloses enzymes and other proteins. BMCs are typically about 40–200 nanometers in diameter and are made entirely of proteins. The shell functions like a membrane, as it is selectively permeable. Other protein-based compartments found in bacteria and archaea include encapsulin nanocompartments and gas vesicles.

<span class="mw-page-title-main">Cob(I)yrinic acid a,c-diamide adenosyltransferase</span> Class of enzymes

In molecular biology, cob(I)yrinic acid a,c-diamide adenosyltransferase EC 2.5.1.17 is an enzyme which catalyses the conversion of cobalamin into one of its coenzyme forms, adenosylcobalamin. Adenosylcobalamin is required as a cofactor for the activity of certain enzymes. AdoCbl contains an adenosyl moiety liganded to the cobalt ion of cobalamin via a covalent Co-C bond.

Inositol-polyphosphate multikinase is an enzyme with systematic name ATP:1D-myo-inositol-1,4,5-trisphosphate 6-phosphotransferase. This enzyme catalyses the following chemical reaction

inositol-1,3,4-trisphosphate 5/6-kinase is an enzyme with systematic name ATP:1D-myo-inositol 1,3,4-trisphosphate 5-phosphotransferase. This enzyme catalyses the following chemical reaction

Propionate kinase is an enzyme with systematic name ATP:propanoate phosphotransferase. This enzyme catalyses the following chemical reaction

References

  1. Fan C, Bobik TA (April 2008). "The PduX enzyme of Salmonella enterica is an L-threonine kinase used for coenzyme B12 synthesis". The Journal of Biological Chemistry. 283 (17): 11322–9. doi: 10.1074/jbc.m800287200 . PMID   18308727.
  2. Fan C, Fromm HJ, Bobik TA (July 2009). "Kinetic and functional analysis of L-threonine kinase, the PduX enzyme of Salmonella enterica". The Journal of Biological Chemistry. 284 (30): 20240–8. doi:10.1074/jbc.m109.027425. PMC   2740450 . PMID   19509296.