Function
Locations
Oxidise L-cysteine to cysteinesulfinate.
Taurine is one of the most abundant free amino acids in mammalian tissues, essential for bile-salt conjugation, osmoregulation, membrane stabilisation, calcium handling and mitochondrial tRNA modification; it is supplied both by endogenous biosynthesis from cysteine and by cellular uptake. The main biosynthetic route starts with cysteine dioxygenase (CDO1), which oxidises L-cysteine to 3-sulfino-L-alanine (cysteinesulfinate) using O2 and a non-heme Fe(II) centre — the committed, rate-limiting step of cysteine catabolism. Cysteinesulfinic acid decarboxylase (CSAD), a PLP-dependent enzyme, then decarboxylates cysteinesulfinate to hypotaurine. A parallel route is provided by 2-aminoethanethiol (cysteamine) dioxygenase (ADO), which oxidises cysteamine (derived from coenzyme A / pantetheine turnover) directly to hypotaurine; ADO is additionally the N-terminal cysteine dioxygenase of the Cys/N-degron oxygen-sensing pathway. Hypotaurine from either route is oxidised to taurine. Cells that synthesise little taurine rely on the plasma-membrane Na+/Cl- -coupled taurine transporter SLC6A6 (TauT) to import it. Defects illustrate the pathway's importance: SLC6A6 loss-of-function causes taurine-deficiency retinal degeneration and cardiomyopathy, and CDO1 is frequently epigenetically silenced in cancer.
All recommended fields populated.
✗ none found
No MODULE:taurine_biosynthesis_and_transport deep-research report alongside the module YAML.
✓ every leaf node grounds to a representative protein.
✓ every declared conforms_to bundle matches its template motif.
✓ every PRECEDES step chains, or its break is acknowledged via chaining_status.
4 complete review(s) · 0 with deep research · 0 missing review · 4 reviewed but lacking deep research
| Gene | Review | Complete | Deep research |
|---|---|---|---|
| ADO Q96SZ5 | ✓ | ✓ | ✗ |
| CDO1 Q16878 | ✓ | ✓ | ✗ |
| CSAD Q9Y600 | ✓ | ✓ | ✗ |
| SLC6A6 P31641 | ✓ | ✓ | ✗ |
Taurine / hypotaurine biosynthesis and transport (GO:0042412 + GO:0015734), grounded to four completed human gene reviews. Two biosynthetic routes converge on hypotaurine: (route 1) CDO1 (Q16878 PTHR12918, GO:0017172, non-heme Fe(II), Cys-Tyr cofactor) oxidises L-cysteine -> cysteinesulfinate, then CSAD (Q9Y600 PTHR45677, GO:0004782, PLP) decarboxylates it -> hypotaurine; (route 2) ADO (Q96SZ5 PTHR22966, GO:0047800, non-heme Fe(II)) oxidises cysteamine -> hypotaurine. Hypotaurine is then oxidised to taurine (the terminal oxidation lacks a firmly assigned human enzyme, so it is not modelled as a node). SLC6A6 (P31641 PTHR11616, GO:0005369, Na+/Cl- symport) imports taurine at the plasma membrane, dominating supply in low-synthesis tissues (retina, heart). ADO is dual-function: besides cysteamine dioxygenase it is the Cys/N-degron N-terminal cysteine dioxygenase oxygen sensor (peptidyl-cysteine oxidation; a proposed_new_ term for the protein-N-terminal-cysteine-dioxygenase MF was noted in the ADO review, since GO lacks a dedicated class). CDO1 is a frequently-silenced tumour suppressor; SLC6A6 LOF -> taurine-deficiency retinal degeneration/cardiomyopathy. GO term ids/labels verified against the local go.db; module passes structural + term-label validation.
Oxidise L-cysteine to cysteinesulfinate.
Decarboxylate cysteinesulfinate to hypotaurine.
Oxidise cysteamine to hypotaurine (alternative route).
Import extracellular taurine into the cytosol (Na+/Cl- symport).