KEGG   ENZYME: 4.4.1.22Help
Entry
EC 4.4.1.22                 Enzyme                                 
Name S-(hydroxymethyl)glutathione synthase;
glutathione-dependent formaldehyde-activating enzyme;
Gfa;
S-(hydroxymethyl)glutathione formaldehyde-lyase
Class Lyases;
Carbon-sulfur lyases;
Carbon-sulfur lyases (only sub-subclass identified to date)
BRITE hierarchy
Sysname S-(hydroxymethyl)glutathione formaldehyde-lyase
(glutathione-forming)
Reaction(IUBMB) S-(hydroxymethyl)glutathione = glutathione + formaldehyde
[RN:R06982]
Reaction(KEGG) R06982
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Substrate S-(hydroxymethyl)glutathione [CPD:C14180]
Product glutathione [CPD:C00051];
formaldehyde [CPD:C00067]
Comment The enzyme from Paracoccus denitrificans accelerates the spontaneous
reaction in which the adduct of formaldehyde and glutathione is
formed, i.e. the substrate for EC 1.1.1.284,
S-(hydroxymethyl)glutathione dehydrogenase, in the
formaldehyde-detoxification pathway.
Pathway PATH: ec00680  Methane metabolism
Orthology KO: K03396  S-(hydroxymethyl)glutathione synthase
Genes XCC: XCC3388
XCB: XC_0776
XCA: xccb100_0811(gfa)
XCV: XCV0789
XAC: XAC0735
XOM: XOO_3646
XOP: PXO_04414
VFI: VF_A0007
VFM: VFMJ11_A0021(gfa)
VSA: VSAL_II0213(gfa)
PPR: PBPRB1570
PSB: Psyr_2957
SFR: Sfri_3436
SSE: Ssed_4230
SPL: Spea_0267 Spea_3387
SHL: Shal_3474 Shal_4035
SWD: Swoo_0373
AFE: Lferr_0844
AFR: AFE_0696(gfa)
BAM: Bamb_5797
BAC: BamMC406_5579
BPY: Bphyt_5113
VEI: Veis_4024
MMS: mma_2819
MLO: mlr0874
SME: SM_b20186
SMD: Smed_3930
RET: RHE_PF00400(yhf00120)
REC: RHECIAT_PC0000582
RLE: pRL120526(gfa)
RLT: Rleg2_4920
RLG: Rleg_4832
RHI: NGR_b14630(gfa1) NGR_c19300 NGR_c20490(gfa2)
BJA: blr6216
BRA: BRADO5487(gfa)
BBT: BBta_5971(gfa)
RPC: RPC_0100
RPE: RPE_4679
RSP: RSP_2575
RSH: Rsph17029_1233
RSQ: Rsph17025_1948
RSK: RSKD131_0887
PDE: Pden_0015
ACR: Acry_2793
Taxonomy
Reference
  Authors
  Title


  Journal
  Organism
  Sequence
 1  [PMID:11741920]
Goenrich M, Bartoschek S, Hagemeier CH, Griesinger C, Vorholt JA.
A glutathione-dependent formaldehyde-activating enzyme (Gfa) from
Paracoccus denitrificans detected and purified via two-dimensional
proton exchange NMR spectroscopy.
J. Biol. Chem. 277 (2002) 3069-72.
Paracoccus denitrificans [GN:pde]
PDE: Pden_0015
Other DBs ExplorEnz - The Enzyme Database: 4.4.1.22
IUBMB Enzyme Nomenclature: 4.4.1.22
ExPASy - ENZYME nomenclature database: 4.4.1.22
UM-BBD (Biocatalysis/Biodegradation Database): 4.4.1.22
BRENDA, the Enzyme Database: 4.4.1.22
CAS: 425642-27-9
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