Mammalian D-Cysteine: A new addition to the growing family of biologically relevant D-amino acids

Robin Roychaudhuri

doi:10.1002/chir.23555

Mammalian D-Cysteine: A new addition to the growing family of biologically relevant D-amino acids

Robin Roychaudhuri

School of Medicine

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

Abstract

Mammalian D-Cysteine is racemized from L-cysteine by serine racemase, a pyridoxal phosphate (PLP)-dependent enzyme. Endogenous D-Cysteine plays a role in neural development by inhibiting proliferation of neural progenitor cells (NPCs) via protein kinase B (AKT) signaling mediated by the FoxO family of transcription factors. D-Cysteine binds to Myristoylated Alanine Rich C Kinase Substrate (MARCKS) and alters phosphorylation at Ser 159/163 and its translocation from the membrane. By racemizing serine and cysteine, mammalian serine racemase may play important roles in neural development highlighting its importance in psychiatric disorders.

Original language	English (US)
Journal	Chirality
DOIs	https://doi.org/10.1002/chir.23555
State	Accepted/In press - 2023

Keywords

AKT
D-Cysteine
D-serine
neural progenitor cell
neurodevelopment
proliferation
racemization
serine racemase

ASJC Scopus subject areas

Drug Discovery
Analytical Chemistry
Spectroscopy
Catalysis
Pharmacology
Organic Chemistry

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10.1002/chir.23555

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title = "Mammalian D-Cysteine: A new addition to the growing family of biologically relevant D-amino acids",

abstract = "Mammalian D-Cysteine is racemized from L-cysteine by serine racemase, a pyridoxal phosphate (PLP)-dependent enzyme. Endogenous D-Cysteine plays a role in neural development by inhibiting proliferation of neural progenitor cells (NPCs) via protein kinase B (AKT) signaling mediated by the FoxO family of transcription factors. D-Cysteine binds to Myristoylated Alanine Rich C Kinase Substrate (MARCKS) and alters phosphorylation at Ser 159/163 and its translocation from the membrane. By racemizing serine and cysteine, mammalian serine racemase may play important roles in neural development highlighting its importance in psychiatric disorders.",

keywords = "AKT, D-Cysteine, D-serine, neural progenitor cell, neurodevelopment, proliferation, racemization, serine racemase",

author = "Robin Roychaudhuri",

note = "Funding Information: I acknowledge my mentor Prof. Solomon H. Snyder (Sol) at the Department of Neuroscience, Johns Hopkins University School of Medicine, in whose laboratory my work identified endogenous D‐Cysteine. This silent discovery was the result of multiple brainstorming sessions with Sol. My original work on endogenous mammalian D‐Cysteine was funded by P50 DA044123 to Prof. Solomon H. Snyder. Publisher Copyright: {\textcopyright} 2023 Wiley Periodicals LLC.",

year = "2023",

doi = "10.1002/chir.23555",

language = "English (US)",

journal = "Chirality",

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T1 - Mammalian D-Cysteine

T2 - A new addition to the growing family of biologically relevant D-amino acids

AU - Roychaudhuri, Robin

N1 - Funding Information: I acknowledge my mentor Prof. Solomon H. Snyder (Sol) at the Department of Neuroscience, Johns Hopkins University School of Medicine, in whose laboratory my work identified endogenous D‐Cysteine. This silent discovery was the result of multiple brainstorming sessions with Sol. My original work on endogenous mammalian D‐Cysteine was funded by P50 DA044123 to Prof. Solomon H. Snyder. Publisher Copyright: © 2023 Wiley Periodicals LLC.

PY - 2023

Y1 - 2023

N2 - Mammalian D-Cysteine is racemized from L-cysteine by serine racemase, a pyridoxal phosphate (PLP)-dependent enzyme. Endogenous D-Cysteine plays a role in neural development by inhibiting proliferation of neural progenitor cells (NPCs) via protein kinase B (AKT) signaling mediated by the FoxO family of transcription factors. D-Cysteine binds to Myristoylated Alanine Rich C Kinase Substrate (MARCKS) and alters phosphorylation at Ser 159/163 and its translocation from the membrane. By racemizing serine and cysteine, mammalian serine racemase may play important roles in neural development highlighting its importance in psychiatric disorders.

AB - Mammalian D-Cysteine is racemized from L-cysteine by serine racemase, a pyridoxal phosphate (PLP)-dependent enzyme. Endogenous D-Cysteine plays a role in neural development by inhibiting proliferation of neural progenitor cells (NPCs) via protein kinase B (AKT) signaling mediated by the FoxO family of transcription factors. D-Cysteine binds to Myristoylated Alanine Rich C Kinase Substrate (MARCKS) and alters phosphorylation at Ser 159/163 and its translocation from the membrane. By racemizing serine and cysteine, mammalian serine racemase may play important roles in neural development highlighting its importance in psychiatric disorders.

KW - AKT

KW - D-Cysteine

KW - D-serine

KW - neural progenitor cell

KW - neurodevelopment

KW - proliferation

KW - racemization

KW - serine racemase

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U2 - 10.1002/chir.23555

DO - 10.1002/chir.23555

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C2 - 36890664

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SN - 0899-0042

JO - Chirality

JF - Chirality

ER -

Mammalian D-Cysteine: A new addition to the growing family of biologically relevant D-amino acids

Abstract

Keywords

ASJC Scopus subject areas

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