Last update 01 Nov 2024

GALK1

Last update 01 Nov 2024

Basic Info

Synonyms

Galactokinase, galactokinase 1, Galactose kinase

+ [2]

Introduction

Catalyzes the transfer of a phosphate from ATP to alpha-D-galactose and participates in the first committed step in the catabolism of galactose.

Drugs associated with GALK1

ML152

Target

GALK1

Mechanism

GALK1 inhibitors

Active Org.

National Human Genome Research Institute

Originator Org.

National Human Genome Research Institute

Active Indication

Galactosemias

Inactive Indication-

Drug Highest PhasePreclinical

First Approval Ctry. / Loc.-

First Approval Date20 Jan 1800

Galactosemia(Scenic Biotech)

Target

GALK1

Mechanism

GALK1 inhibitors

Active Org.

Scenic Biotech BVStartup

Originator Org.

Scenic Biotech BVStartup

Active Indication

Galactosemias

Inactive Indication-

Drug Highest PhaseDiscovery

First Approval Ctry. / Loc.-

First Approval Date20 Jan 1800

Galactokinase inhibitors (NIH)

Target

GALK1

Mechanism

GALK1 inhibitors

Active Org.-

Originator Org.

National Institutes of Health

Active Indication-

Inactive Indication

Galactosemias

Drug Highest PhasePending

First Approval Ctry. / Loc.-

First Approval Date20 Jan 1800

100 Clinical Results associated with GALK1

100 Translational Medicine associated with GALK1

0 Patents (Medical) associated with GALK1

1,030

Literatures (Medical) associated with GALK1

01 Dec 2024·Microbiological Research

Unveiling the genetic basis and metabolic rewiring behind the galactose-positive phenotype in a Streptococcus thermophilus mutant

Article

Author: Peng, Qingting ; Lu, Wenhui ; Liu, Jinhui ; Dan, Tong ; Tai, Jiahui ; Hu, Haimin

Streptococcus thermophilus (S. thermophilus) is a widely used starter culture in dairy fermentation, but most strains are galactose-negative and only metabolize glucose from lactose hydrolysis. In this study, we aimed to uncover the mechanisms underlying the acquisition of a stable galactose-positive (Gal⁺) phenotype in a mutant strain of S. thermophilus IMAU10636. By treating the wild-type strain with the mutagenic agent N-methyl-N-nitro-N-nitrosoguanidine, we successfully isolated a Gal⁺ mutant, S. thermophilus IMAU10636Y. Comparative enzyme activity assays revealed that the mutant exhibited higher β-galactosidase and galactokinase activities, but lower glucokinase and pyruvate kinase activities compared to the wild-type. High-performance liquid chromatography analysis confirmed the mutant's enhanced ability to utilize lactose and galactose, leading to increased glucose secretion. Integrated genome and transcriptomics analyses provided deeper insights into the underlying genetic and metabolic mechanisms. We found that the metabolism regulatory network of the glycolysis / Leloir pathway was altered in the mutant, possibly due to the upregulation of the gene expression in the galR-galK intergenic region. This likely led to increased RNA polymerase binding and transcription of the gal operon, ultimately promoting the Gal⁺ phenotype. Additionally, we identified a mutation in the scrR gene, encoding a LacI family transcriptional repressor, which also contributed to the Gal⁺ phenotype. These findings offer new perspectives on the metabolic rewiring and regulatory mechanisms that enable S. thermophilus to acquire the ability to metabolize galactose. This knowledge can inform strategies for engineering and selecting Gal⁺ strains with desirable fermentation characteristics for dairy applications.

09 Oct 2024·Journal of Agricultural and Food Chemistry

Unlocking Industrial Potential: Phase-Transition Coimmobilization of Multienzyme Systems for High-Efficiency Uridine Diphosphate Galactose Production

Article

Author: Li, Yajing ; Yang, Xinrui ; Li, Yuejun ; Chen, Qi ; Gao, Renjun

Transitioning from batch to continuous industrial production often improves the economic returns and production efficiency. Immobilization is a critical strategy that can facilitate this shift. This study refined the previously established method for synthesizing uridine diphosphate galactose (UDP-Gal) by employing thermophilic enzymes. Three thermophilic enzymes (galactokinase, uridine diphosphate glucose pyrophosphorylase, and inorganic pyrophosphatase) were coimmobilized on the pH-responsive carrier Eudragit S-100, promoting enzyme recovery and reuse while their industrial potential was assessed. The coimmobilization system efficiently catalyzed UDP-Gal production, yielding 13.69 mM in 1.5 h, attaining a UTP conversion rate of 91.2% and a space-time yield (STY) of 5.16 g/L/h. Moreover, the system exhibited exceptional reproducibility, retaining 58.9% of its initial activity after five cycles. This research highlighted promising prospects for coimmobilization in industrial synthesis and proposed a novel methodology for enhancing UDP-Gal production in the industry. In addition, the phase-transition property of Eudragit S-100 paves the way for further exploration with the one-pot synthesis of poorly soluble galactosides.

01 Aug 2024·Biochimie

Galactokinase-like protein from Leishmania donovani: Biochemical and structural characterization of a recombinant protein

Article

Author: Aghajani, Arega ; Winter, Anja ; Hyatt, James G ; Maciej-Hulme, Marissa L ; Sari, Suat ; Price, Helen P ; Bethel, Cassandra ; Baber, Hasana ; Gallimore, B Harold ; King, Elizabeth F B

Leishmaniasis is a spectrum of conditions caused by infection with the protozoan Leishmania spp. parasites. Leishmaniasis is endemic in 98 countries around the world, and resistance to current anti-leishmanial drugs is rising. Our work has identified and characterised a previously unstudied galactokinase-like protein (GalK) in Leishmania donovani, which catalyses the MgATP-dependent phosphorylation of the C-1 hydroxyl group of d-galactose to galactose-1-phosphate. Here, we report the production of the catalytically active recombinant protein in E. coli, determination of its substrate specificity and kinetic constants, as well as analysis of its molecular envelope using in solution X-ray scattering. Our results reveal kinetic parameters in range with other galactokinases with an average apparent Km value of 76 μM for galactose, V_max and apparent K_cat values with 4.46376 × 10^-9 M/s and 0.021 s^-1, respectively. Substantial substrate promiscuity was observed, with galactose being the preferred substrate, followed by mannose, fructose and GalNAc. LdGalK has a highly flexible protein structure suggestive of multiple conformational states in solution, which may be the key to its substrate promiscuity. Our data presents novel insights into the galactose salvaging pathway in Leishmania and positions this protein as a potential target for the development of pharmaceuticals seeking to interfere with parasite substrate metabolism.

Analysis

Perform a panoramic analysis of this field.

view full example data

Chat with Hiro

Get started for free today!

Accelerate Strategic R&D decision making with Synapse, PatSnap’s AI-powered Connected Innovation Intelligence Platform Built for Life Sciences Professionals.

Start your data trial now!

Synapse data is also accessible to external entities via APIs or data packages. Empower better decisions with the latest in pharmaceutical intelligence.

Bio

Bio Sequences Search & Analysis

Chemical

Chemical Structures Search & Analysis

GALK1

Basic Info

Related

Analysis