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Information on EC 2.8.1.16 - L-aspartate semialdehyde sulfurtransferase and Organism(s) Methanocaldococcus jannaschii and UniProt Accession Q57564

for references in articles please use BRENDA:EC2.8.1.16
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IUBMB Comments
The enzyme, characterized from the archaeon Methanosarcina acetivorans, participates in an L-methionine biosysnthetic pathway found in most of the methanogenic archaea.
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Methanocaldococcus jannaschii
UNIPROT: Q57564
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The taxonomic range for the selected organisms is: Methanocaldococcus jannaschii
The enzyme appears in selected viruses and cellular organisms
Reaction Schemes
+
+
2
reduced ferredoxin [iron-sulfur] cluster
+
2
=
+
+
2
oxidized ferredoxin [iron-sulfur] cluster
Synonyms
mj0100, ma1821, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
MA1821
-
-
-
-
PATHWAY SOURCE
PATHWAYS
-
-
SYSTEMATIC NAME
IUBMB Comments
hydrogen sulfide:L-aspartate-4-semialdehyde sulfurtransferase
The enzyme, characterized from the archaeon Methanosarcina acetivorans, participates in an L-methionine biosysnthetic pathway found in most of the methanogenic archaea.
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
hydrogen sulfide + L-aspartate 4-semialdehyde + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+
L-homocysteine + H2O + 2 oxidized ferredoxin [iron-sulfur] cluster
show the reaction diagram
-
-
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
hydrogen sulfide + L-aspartate 4-semialdehyde + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+
L-homocysteine + H2O + 2 oxidized ferredoxin [iron-sulfur] cluster
show the reaction diagram
-
-
-
?
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
26000
recombinant CBS-domain pair, residues 381-509
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
dimer
dynamic light scattering, isolated CBS-domain pair, residues 381-509
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
structure of the isolated CBS-domain pair, residues 381-509, both native and selenomethionine-substituted protein. Space group P212121, unit cell parameters a 80.9, b 119.5, c 173.3 A
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression of the CBS-domain pair, residues 381-509 in Escherichia coli
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Lucas, M.; Kortazar, D.; Astigarraga, E.; Fernandez, J.A.; Mato, J.M.; Martinez-Chantar, M.L.; Martinez-Cruz, L.A.
Purification, crystallization and preliminary X-ray diffraction analysis of the CBS-domain pair from the Methanococcus jannaschii protein MJ0100
Acta Crystallogr. Sect. F
64
936-941
2008
Methanocaldococcus jannaschii (Q57564), Methanocaldococcus jannaschii, Methanocaldococcus jannaschii ATCC 43067 (Q57564)
Manually annotated by BRENDA team
Allen, K.; Miller, D.; Rauch, B.; Perona, J.; White, R.
Homocysteine is biosynthesized from aspartate semialdehyde and hydrogen sulfide in methanogenic archaea
Biochemistry
54
3129-3132
2015
Methanocaldococcus jannaschii (Q57564), Methanocaldococcus jannaschii ATCC 43067 (Q57564), Methanosarcina acetivorans (Q8TPT4), Methanosarcina acetivorans DSM 2834 (Q8TPT4)
Manually annotated by BRENDA team