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Information on EC 4.6.1.2 - guanylate cyclase and Organism(s) Chlamydomonas reinhardtii and UniProt Accession Q5YLC2

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IUBMB Comments
Also acts on ITP and dGTP.
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This record set is specific for:
Chlamydomonas reinhardtii
UNIPROT: Q5YLC2
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The taxonomic range for the selected organisms is: Chlamydomonas reinhardtii
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea
Synonyms
guanylate cyclase, soluble guanylate cyclase, guanylyl cyclase, soluble guanylyl cyclase, npr-a, npr-b, particulate guanylate cyclase, h-nox, no receptor, guanylyl cyclase c, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
soluble guanylate cyclase
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ANPRA
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ANPRB
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Atrial natriuretic peptide A-type receptor
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-
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Atrial natriuretic peptide B-type receptor
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guanyl cyclase
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Guanylate cyclase
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-
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Guanylate cyclase 2D, retinal
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Guanylate cyclase 2E
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Guanylate cyclase 2F, retinal
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Guanylate cyclase, olfactory
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guanylyl cyclase
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hSTAR
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Intestinal guanylate cyclase
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KSGC
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Rod outer segment membrane guanylate cyclase
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ROS-GC
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ROS-GC2
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STA receptor
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
P-O bond cleavage
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-
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PATHWAY SOURCE
PATHWAYS
SYSTEMATIC NAME
IUBMB Comments
GTP diphosphate-lyase (cyclizing; 3',5'-cyclic-GMP-forming)
Also acts on ITP and dGTP.
CAS REGISTRY NUMBER
COMMENTARY hide
9054-75-5
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SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
GTP
3',5'-cyclic GMP + diphosphate
show the reaction diagram
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-
-
?
additional information
?
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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
GTP
3',5'-cyclic GMP + diphosphate
show the reaction diagram
-
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
heme
in soluble guanylate cyclases
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Mn2+
most effective, Mg2+ activates to 1% of the activity with Mn2+
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
additional information
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
soluble isozyme; gene CYG12 encoding the soluble isozyme
UniProt
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
soluble guanylate cyclase
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Manually annotated by BRENDA team
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
Q5YLC2_CHLRE
991
0
106435
TrEMBL
other Location (Reliability: 5)
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
dimer
catalytic domain, crystal structure, structure analysis and comparison, e.g. of helix alpha1, modelling, overview
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
isolated dimeric and inactive catalytic domain, X-ray diffraction structure determination and analysis at 2.55 A resolution
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
gene CYG12 encodes the soluble isozyme
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Winger, J.A.; Derbyshire, E.R.; Lamers, M.H.; Marletta, M.A.; Kuriyan, J.
The crystal structure of the catalytic domain of a eukaryotic guanylate cyclase
BMC Struct. Biol.
8
42
2008
Chlamydomonas reinhardtii (Q5YLC2), Chlamydomonas reinhardtii
Manually annotated by BRENDA team