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Erwinia asparaginase

Andrew E. Place, MD · FDA-approved active Small molecule

Erwinia asparaginase depletes the amino acid asparagine in the bloodstream, starving leukemic cells that cannot synthesize their own asparagine.

Erwinia asparaginase depletes the amino acid asparagine in the bloodstream, starving leukemic cells that cannot synthesize their own asparagine. Used for Acute lymphoblastic leukemia (ALL), as part of combination chemotherapy regimens, Acute myeloid leukemia (AML), in select cases.

At a glance

Generic nameErwinia asparaginase
Also known asRylze or native Erwinia asparaginase, Erwinase®, ERWINAZE®, ERWINIA CHRYSANTHEMI, ERWINASE®
SponsorAndrew E. Place, MD
Drug classEnzyme
TargetAsparagine
ModalitySmall molecule
Therapeutic areaOncology
PhaseFDA-approved

Mechanism of action

Asparaginase is an enzyme that catalyzes the hydrolysis of asparagine to aspartic acid and ammonia. Acute lymphoblastic leukemia (ALL) cells are dependent on exogenous asparagine for protein synthesis and survival, whereas normal cells can synthesize asparagine endogenously. By depleting circulating asparagine, the enzyme selectively inhibits leukemic cell growth. Erwinia asparaginase is derived from the bacterium Erwinia chrysanthemi and is used as an alternative to E. coli asparaginase, particularly in patients who develop hypersensitivity to the E. coli formulation.

Approved indications

Common side effects

Key clinical trials

Primary sources

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SourceUsed for
ClinicalTrials.govTrial enrolment, design, endpoints, results

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