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DraconiticBiochemistryBiomolecules · Catabolism · Biosynthesis · MetabolismMap

Data

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Human metabolism

Reactome's human metabolism drawn as one network. Each molecule has one home node; widely shared molecules also appear as dashed copies in other territories, linked from their details. .

Territories

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Metabolite; its structure appears as you zoom in
Reaction, arrow toward the product
Cofactors and co-substrates are written beside the reaction when you zoom in
Dashed ring: a copy of a widely shared molecule or cofactor in another territory or pathway
Compartment transfer of the molecule it is linked to
Binding, release or complex event; its proteins are named in its details
Outline: reactions mostly in the mitochondrion

Arrows follow Reactome's curated reaction direction.

ASS1 tetramer:NMRAL1 dimer:NADPH transforms L-Asp and L-Cit to ARSUA

ATP + L-Asp + L-Cit → ARSUA + AMP + PPi + H+

Reactome: R-HSA-70577
Compartment: cytosol
Rhea: RHEA:10933

Inputs

ATPCHEBI:30616, C10H12N5O13P3, cytosol
L-AspCHEBI:29991, C4H6NO4, cytosol
L-CitCHEBI:57743, C6H13N3O3, cytosol

Outputs

ARSUACHEBI:57472, C10H17N4O6, cytosol
AMPCHEBI:456215, C10H12N5O7P, cytosol
PPiCHEBI:33019, HO7P2, cytosol
H+CHEBI:15378, H, cytosol

Catalysed by

argininosuccinate synthase activity of ASS1 tetramer:NMRAL1 dimer:NADPH [cytosol]EC 6.3.4.5

Literature

Mutations and polymorphisms in the human argininosuccinate synthetase (ASS1) gene Hum Mutat, 2009
Structure of human argininosuccinate synthetase Acta Crystallogr D Biol Crystallogr, 2008
Isolation and characterization of argininosuccinate synthetase from human liver. Biochemistry, 1980
Restructuring of the dinucleotide-binding fold in an NADP(H) sensor protein Proc. Natl. Acad. Sci. U.S.A., 2007
An NADPH sensor protein (HSCARG) down-regulates nitric oxide synthesis by association with argininosuccinate synthetase and is essential for epithelial cell viability J. Biol. Chem., 2008