BRENDA - Enzyme Database show
show all sequences of 4.99.1.4

Structural diversity in metal ion chelation and the structure of uroporphyrinogen III synthase

Schubert, H.L.; Raux, E.; Matthews, M.A.; Phillips, J.D.; Wilson, K.S.; Hill, C.P.; Warren, M.J.; Biochem. Soc. Trans. 30, 595-600 (2002)

Data extracted from this reference:

Crystallization (Commentary)
Crystallization
Organism
X-ray crystal structure of Met8p
Saccharomyces cerevisiae
Engineering
Amino acid exchange
Commentary
Organism
D141A
mutant of bifunctional Met8p is devoid of both dehydrogenase and ferrochelatase activities
Saccharomyces cerevisiae
G22D
mutant of bifunctional Met8p is completely inactive as NAD+-dependent dehydrogenase, but functions as ferrochelatase
Saccharomyces cerevisiae
Natural Substrates/ Products (Substrates)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
sirohydrochlorin + Fe2+
Saccharomyces cerevisiae
Met8p catalyzes ferrochelation during the biosynthesis of siroheme
siroheme + 2 H+
-
Saccharomyces cerevisiae
?
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Saccharomyces cerevisiae
-
-
-
Reaction
Reaction
Commentary
Organism
siroheme + 2 H+ = sirohydrochlorin + Fe2+
the enzyme from Pseudomonas chloroaphis contains Ca2+ and protoheme IX, the iron of which must be in the form Fe2+ for activity, the enzyme exhibits a strong preference for aliphatic aldoximes, such as butyraldoxime and acetaldoxime, over aromatic aldoximes, such as pyridine-2-aldoxime, which is a poor substrate, no activity was found with the aromatic aldoximes benzaldoxime and pyridine-4-aldoxime, mechanism
Saccharomyces cerevisiae
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
sirohydrochlorin + Fe2+
Met8p catalyzes ferrochelation during the synthesis of siroheme, both ferrochelation and NAD+-dependent dehydrogenation of preccorin-2 to produce sirohydrochlorin take place in a single bifunctional active site, Asp-141 participates in both catalytic reactions, which are not linked mechanistically, mechanism
649817
Saccharomyces cerevisiae
siroheme + 2 H+
-
649817
Saccharomyces cerevisiae
?
sirohydrochlorin + Fe2+
Met8p catalyzes ferrochelation during the biosynthesis of siroheme
649817
Saccharomyces cerevisiae
siroheme + 2 H+
-
649817
Saccharomyces cerevisiae
?
Subunits
Subunits
Commentary
Organism
homodimer
each monomer is composed of three functional domains, domain structure
Saccharomyces cerevisiae
Crystallization (Commentary) (protein specific)
Crystallization
Organism
X-ray crystal structure of Met8p
Saccharomyces cerevisiae
Engineering (protein specific)
Amino acid exchange
Commentary
Organism
D141A
mutant of bifunctional Met8p is devoid of both dehydrogenase and ferrochelatase activities
Saccharomyces cerevisiae
G22D
mutant of bifunctional Met8p is completely inactive as NAD+-dependent dehydrogenase, but functions as ferrochelatase
Saccharomyces cerevisiae
Natural Substrates/ Products (Substrates) (protein specific)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
sirohydrochlorin + Fe2+
Saccharomyces cerevisiae
Met8p catalyzes ferrochelation during the biosynthesis of siroheme
siroheme + 2 H+
-
Saccharomyces cerevisiae
?
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
sirohydrochlorin + Fe2+
Met8p catalyzes ferrochelation during the synthesis of siroheme, both ferrochelation and NAD+-dependent dehydrogenation of preccorin-2 to produce sirohydrochlorin take place in a single bifunctional active site, Asp-141 participates in both catalytic reactions, which are not linked mechanistically, mechanism
649817
Saccharomyces cerevisiae
siroheme + 2 H+
-
649817
Saccharomyces cerevisiae
?
sirohydrochlorin + Fe2+
Met8p catalyzes ferrochelation during the biosynthesis of siroheme
649817
Saccharomyces cerevisiae
siroheme + 2 H+
-
649817
Saccharomyces cerevisiae
?
Subunits (protein specific)
Subunits
Commentary
Organism
homodimer
each monomer is composed of three functional domains, domain structure
Saccharomyces cerevisiae
Other publictions for EC 4.99.1.4
No.
1st author
Pub Med
title
organims
journal
volume
pages
year
Activating Compound
Application
Cloned(Commentary)
Crystallization (Commentary)
Engineering
General Stability
Inhibitors
KM Value [mM]
Localization
Metals/Ions
Molecular Weight [Da]
Natural Substrates/ Products (Substrates)
Organic Solvent Stability
Organism
Oxidation Stability
Posttranslational Modification
Purification (Commentary)
Reaction
Renatured (Commentary)
Source Tissue
Specific Activity [micromol/min/mg]
Storage Stability
Substrates and Products (Substrate)
Subunits
Temperature Optimum [°C]
Temperature Range [°C]
Temperature Stability [°C]
Turnover Number [1/s]
pH Optimum
pH Range
pH Stability
Cofactor
Ki Value [mM]
pI Value
IC50 Value
Activating Compound (protein specific)
Application (protein specific)
Cloned(Commentary) (protein specific)
Cofactor (protein specific)
Crystallization (Commentary) (protein specific)
Engineering (protein specific)
General Stability (protein specific)
IC50 Value (protein specific)
Inhibitors (protein specific)
Ki Value [mM] (protein specific)
KM Value [mM] (protein specific)
Localization (protein specific)
Metals/Ions (protein specific)
Molecular Weight [Da] (protein specific)
Natural Substrates/ Products (Substrates) (protein specific)
Organic Solvent Stability (protein specific)
Oxidation Stability (protein specific)
Posttranslational Modification (protein specific)
Purification (Commentary) (protein specific)
Renatured (Commentary) (protein specific)
Source Tissue (protein specific)
Specific Activity [micromol/min/mg] (protein specific)
Storage Stability (protein specific)
Substrates and Products (Substrate) (protein specific)
Subunits (protein specific)
Temperature Optimum [°C] (protein specific)
Temperature Range [°C] (protein specific)
Temperature Stability [°C] (protein specific)
Turnover Number [1/s] (protein specific)
pH Optimum (protein specific)
pH Range (protein specific)
pH Stability (protein specific)
pI Value (protein specific)
Expression
General Information
General Information (protein specific)
Expression (protein specific)
KCat/KM [mM/s]
KCat/KM [mM/s] (protein specific)
748869
Garai
Phylogenetic analysis and pho ...
Arabidopsis thaliana
Physiol. Mol. Biol. Plants
22
351-359
2016
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
3
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
3
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
1
-
-
730419
Bali
Identification and characteriz ...
Paracoccus pantotrophus
Mol. Microbiol.
92
153-163
2014
-
-
1
1
-
-
-
-
-
-
1
1
-
1
-
-
1
-
-
-
-
-
1
1
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
1
-
-
-
-
-
-
-
-
1
1
-
-
-
1
-
-
-
-
1
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
729160
Saha
Characterization of the evolut ...
Arabidopsis thaliana
Biochem. J.
444
227-237
2012
-
-
1
-
5
-
-
-
1
1
2
1
-
5
-
-
1
-
-
1
6
-
1
1
-
-
-
-
-
-
-
1
-
-
-
-
-
1
1
-
5
-
-
-
-
-
1
1
2
1
-
-
-
1
-
1
6
-
1
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
716791
Romao
Evolution in a family of chela ...
Bacillus megaterium
Proc. Natl. Acad. Sci. USA
108
97-102
2011
-
-
-
-
-
-
-
-
-
-
-
1
-
1
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
696120
Lobo
Functional characterization of ...
no activity in Desulfovibrio vulgaris
Biochem. J.
420
317-325
2009
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
665692
Raux-Deery
Identification and characteriz ...
Arabidopsis thaliana
J. Biol. Chem.
280
4713-4721
2005
-
-
1
-
-
-
2
1
1
2
-
1
-
4
-
-
1
-
-
-
2
-
3
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
2
-
1
1
2
-
1
-
-
-
1
-
-
2
-
3
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
649745
Raux
Identification and functional ...
Bacillus megaterium, Bacillus megaterium DSM 509
Biochem. J.
370
505-516
2003
-
-
1
-
-
-
-
-
1
-
1
2
-
4
-
-
1
-
-
-
2
-
8
1
-
-
-
-
1
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
1
-
1
2
-
-
-
1
-
-
2
-
8
1
-
-
-
-
1
-
-
-
-
-
-
-
-
-
653297
Stroupe
CysG structure reveals tetrapy ...
Salmonella enterica
Nat. Struct. Biol.
10
1064-1073
2003
-
-
1
1
2
-
-
-
-
-
-
1
-
1
-
1
1
-
-
-
3
-
3
1
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
1
2
-
-
-
-
-
-
-
-
1
-
-
1
1
-
-
3
-
3
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
644283
Schubert
The structure of Saccharomyces ...
Saccharomyces cerevisiae
EMBO J.
21
2068-2075
2002
-
-
1
1
3
-
-
-
-
-
-
2
-
2
-
-
1
-
-
-
2
-
4
1
-
-
-
-
1
-
-
-
-
-
-
-
-
1
-
1
3
-
-
-
-
-
-
-
-
2
-
-
-
1
-
-
2
-
4
1
-
-
-
-
1
-
-
-
-
-
-
-
-
-
649817
Schubert
Structural diversity in metal ...
Saccharomyces cerevisiae
Biochem. Soc. Trans.
30
595-600
2002
-
-
-
1
2
-
-
-
-
-
-
1
-
1
-
-
-
1
-
-
-
-
2
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
2
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
2
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-