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Last update 08 May 2025

SRR

Last update 08 May 2025

Basic Info

Synonyms

D-serine ammonia-lyase, D-serine dehydratase, ILV1

+ [5]

Introduction

Catalyzes the synthesis of D-serine from L-serine (PubMed:20106978, PubMed:23391306, PubMed:29277459). D-serine is a key coagonist with glutamate at NMDA receptors. Has dehydratase activity towards both L-serine and D-serine (By similarity).

Drugs associated with SRR

SRR inhibitors(ASCR)

Target

SRR

Mechanism

SRR inhibitors

Active Org.-

Originator Org.-

Active Indication

Peripheral Nervous System Diseases

Inactive Indication-

Drug Highest PhasePreclinical

First Approval Ctry. / Loc.-

First Approval Date20 Jan 1800

Serine Racemase Inhibitor(University of Parma)

Target

SRR

Mechanism

SRR inhibitors

Active Org.

University of Parma

Originator Org.-

Active Indication

Neurodegenerative Diseases

Inactive Indication-

Drug Highest PhasePreclinical

First Approval Ctry. / Loc.-

First Approval Date20 Jan 1800

Clinical Trials associated with SRR

ChiCTR2500096387

/ SuspendedNot ApplicableIIT

A prospective, multi-center, randomized, subject- and evaluator-blinded, active-controlled clinical trial to evaluate the safety and effectiveness of PRECISE-HA Filler LIPS for enhancement of lip volume and shape in Chinese population

Start Date23 Jul 2024

Sponsor / Collaborator-

NCT06499753

/ CompletedNot ApplicableIIT

Differences in Dry Eye Symptoms Related to Geographic Location in Spain and Impact of Artificial Tears Use

This study assessed the differences in DED symptomatology measured with the OSDI questionnaire regarding climate data of the geographic location in a large population in Spain, with a special focus on the relative humidity (RH) of the place of residence and the impact of artificial tears use, to help eye care practitioners in patient management and education

Start Date01 Feb 2020

Sponsor / Collaborator

University of Valladolid

100 Clinical Results associated with SRR

100 Translational Medicine associated with SRR

0 Patents (Medical) associated with SRR

1,079

Literatures (Medical) associated with SRR

01 Jul 2025·Journal of Microbiological Methods

Development of novel and efficient Corynebacterium glutamicum gene expression systems for industrial enzyme production

Article

Author: Wu, Ziqi ; Xu, Daqing ; Wang, Miao ; Wu, Liqiang ; Ren, Xiaoxin

An ideal microbial gene expression system for industrial enzyme production should possess a function complementary selection marker, a cost-effective inducer, and the ability for extracellular protein secretion. In this study，we employed CRISPR-Cpf1 gene editing technology to construct an engineered Corynebacterium glutamicum host strain, C. glutamicum Δalr∷araE ΔmurI, by deleting the alanine racemase-encoding gene alr and the glutamate racemase-encoding gene murI, and by integrating the Bacillus subtilis arabinose-related compounds permease-encoding gene araE into the chromosome. The two secretion-type expression vectors pAU30S (Sec-type) and pAU30T (Tat-type) that both employ alr as selection marker, the T7 transcription system to transcribe target genes, and the B. subtilis AraR-OR_A1/OR_A2 negative control system to control gene transcription, were constructed. The α-amylase AmyF from Geobacillus stearothermophilus was used as reporter protein to test the applicability of the L-arabinose-induced gene expression systems C. glutamicum/pAU30S and C. glutamicum Δalr∷araE ΔmurI/pAU30T. The results of transparent circle investigation, SDS-PAGE and amylase activity analysis demonstrated that the recombinant AmyF was efficiently expressed and completely secreted into the culture medium in its active form. The C. glutamicum Δalr∷araE ΔmurI/pAU30S and C. glutamicum Δalr∷araE ΔmurI/pAU30T systems represent highly efficient gene expression platforms suitable for the secretory production of industrial enzymes.

01 Apr 2025·Research in Microbiology

Transposition of transposable element IS1 in Edwardsiella piscicida mutant generated by CRISPR/Cas9 along with λ-Red recombineering system

Article

Author: Kim, Ki Hong ; Lee, Eun Gyeong

This study aimed to investigate unintended mutations introduced by the CRISPR/Cas9 genome editing system in Edwardsiella piscicida. Whole-genome sequencing was conducted on the wild-type E. piscicida NH1 and its alanine racemase knockout mutants (E. piscicida Δalr325 NH1 and E. piscicida Δalr50 NH1) generated using CRISPR/Cas9 with a λ-Red recombineering system. Comparative genomic analyses revealed that the insertion sequence 1 (IS1) transpositions occurred in the CRISPR/Cas9-edited mutants, disrupting the type I restriction-modification system subunit M gene, in addition to the targeted gene deletion. Interestingly, no IS1 transpositions were detected in mutants produced via conventional plasmid-based allelic exchange, indicating the potential link between CRISPR/Cas9-mediated editing and transposition events. These results suggest that genome editing via CRISPR/Cas9 could trigger IS1 transposition, potentially due to double-stranded DNA breaks. The lack of sequence similarity between the single guide RNA (sgRNA) and the transposed regions suggests that transpositions are not CRISPR/Cas9 off-target effects. This study provides evidence of interactions between mobile genetic elements and genome editing systems, requiring further investigation into their underlying mechanisms.

10 Mar 2025·Journal of Chemical Information and Modeling

Mechanistic Insights into the Reversible Inhibition of d-Cycloserine in Alanine Racemase from Mycobacterium tuberculosis

Article

Author: Yang, Wei ; Zhuang, Jingyuan ; Cheng, Gui-Juan

d-Cycloserine (DCS), an antibiotic used in the treatment of drug-resistant tuberculosis, was traditionally believed to irreversibly inhibit the pyridoxal-5'-phosphate (PLP)-dependent alanine racemase from Mycobacterium tuberculosis (MtAlr). However, recent research suggests that the inhibition is reversible, as MtAlr can be reactivated by destructing DCS. This study employs the hybrid quantum mechanics/molecular mechanics (QM/MM) method to investigate the mechanisms of MtAlr inhibition and DCS destruction. Computational results indicate that the inhibition reaction via an "isoxazole-forming" pathway is kinetically favorable, while the DCS destruction reaction via an "oxime-forming" pathway is thermodynamically favorable, explaining the irreversible inhibition of DCS. For the inhibition reaction, the isoxazole product was found to prefer the keto form, contrary to the previously proposed enol form. Moreover, K44 and D322' were identified as key residues. K44 transfers the proton from Cα and Cβ of DCS, while D322' stabilizes the carbanion intermediate and isoxazole product via electrostatic interaction with the protonated K44. Such electrostatic interaction was eliminated in the DCS-resistance variant, D322'N, making the inhibition reaction unfavorable. For DCS destruction, an "up-to-down" conformational change is required to place the isoxazolidinone ring in an appropriate position for hydrolysis. The deprotonated Y273' facilitates the hydrolysis reaction by enhancing the nucleophilicity of the water molecule. Throughout the whole reaction of MtAlr, PLP plays multiple roles, including stabilizing the carbanion intermediate and acting as a proton shuttle. Overall, this study provides deeper insight into the catalytic mechanism of MtAlr and offers valuable insights for drug development.

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