Structure and catalytic mechanism of N(5),N(10)-methenyl-tetrahydromethanopterin cyclohydrolase.

@article{Upadhyay2012StructureAC,
  title={Structure and catalytic mechanism of N(5),N(10)-methenyl-tetrahydromethanopterin cyclohydrolase.},
  author={Vikrant Upadhyay and Ulrike Demmer and Eberhard Warkentin and Johanna Moll and Seigo Shima and Ulrich Ermler},
  journal={Biochemistry},
  year={2012},
  volume={51 42},
  pages={
          8435-43
        }
}
Methenyltetrahydromethanopterin (methenyl-H(4)MPT(+)) cyclohydrolase (Mch) catalyzes the interconversion of methenyl-H(4)MPT(+) and formyl-H(4)MPT in the one-carbon energy metabolism of methanogenic, methanotrophic, and sulfate-reducing archaea and of methylotrophic bacteria. To understand the catalytic mechanism of this reaction, we kinetically characterized site-specific variants of Mch from Archaeoglobus fulgidus (aMch) and determined the X-ray structures of the substrate-free aMch(E186Q… 
View on PubMed
doi.org
9 Citations
Background Citations
1

Figures and Tables from this paper

9 Citations

The crystal structure of archaeal serine hydroxymethyltransferase reveals idiosyncratic features likely required to withstand high temperatures
TLDR
The hypothesis that removal of frustrated interactions (such as the Arg‐Tyr cation‐π interaction occurring in mesophile SHMTs) is an additional strategy of adaptation to high temperature is formed.
The crystal structure of methenyltetrahydromethanopterin cyclohydrolase from Methanobrevibacter ruminantium
TLDR
Sequence and structural alignments have helped identify residues involved in substrate binding and trimer formation inhenyltetrahydromethanopterin cyclohydrolase.
Complexome analysis of the nitrite-dependent methanotroph Methylomirabilis lanthanidiphila.
Metal enzymes in "impossible" microorganisms catalyzing the anaerobic oxidation of ammonium and methane.
TLDR
Understanding is only emerging how hydrazine synthase and the NO dismutase act, it seems clear that reactions fully rely on metal-based catalyses known from other enzymes, and Metal-dependent conversions not only hold for these key enzymes, but for most other reactions in the central catabolic pathways.
Potential and existing mechanisms of enteric methane production in ruminants
TLDR
Research efforts to understand the methanogenesis mechanism should focus on isolation and identification of more specific methanogens, and their genome sequences to provide benefits in terms of improved dietary energy utilization and a reduced contribution of enteric CH4 emissions to total global greenhouse gas emissions from the ruminant production system.
Analysis of a novel protein in human colorectal adenocarcinoma.
TLDR
A novel protein, which may be involved in nuclear signal transduction, was identified using bioinformatics, mass spectrometry and western blot analysis and its function in adenocarcinoma was explored.
Structural insight into a molecular mechanism of methenyltetrahydrofolate cyclohydrolase from Methylobacterium extorquens AM1.
Hydrogenotrophic Methanogenesis
The crystal structure of methenyltetrahyd romethanopterin cyclohydrolase from Methanobrevibacter

References

SHOWING 1-10 OF 60 REFERENCES
The crystal structure of methenyltetrahydromethanopterin cyclohydrolase from the hyperthermophilic archaeon Methanopyrus kandleri.
Methenyl-tetrahydromethanopterin cyclohydrolase in cell extracts of Methanobacterium.
How an Enzyme Binds the C1 Carrier Tetrahydromethanopterin
TLDR
The structure of the homopentameric formaldehyde-activating enzyme (Fae) from Methylobacterium extorquens AM1 is described and methylene-H4MPT, an essential enzyme for energy metabolism and formaldehyde detoxification of this bacterium, shows a characteristic kink between the tetrahydropyrazine and the imidazolidine rings of 70°.
A methenyl tetrahydromethanopterin cyclohydrolase and a methenyl tetrahydrofolate cyclohydrolase in Methylobacterium extorquens AM1.
TLDR
Based on the specific activities in cell extract and from the growth properties of insertion mutants it is suggested that the methenyl H4MPT cyclohydrolase might have a catabolic function in the C1-unit metabolism of M. extorquens AM1.
Purification and properties of 5,10-methenyltetrahydromethanopterin cyclohydrolase from Methanosarcina barkeri
TLDR
The 5,10-methenyltetrahydromethanopterin cyclohydrolase from Methanosarcina barkeri was purified 313-fold to a specific activity of 470 mumol min-1 mg-1 at 37 degrees C and pH 7.8 and the monofunctional enzyme was oxygen stable, but the presence of a detergent proved to be essential for its stability.
N5,N10-Methenyltetrahydromethanopterin cyclohydrolase from the extreme thermophile Methanopyrus kandleri: increase of catalytic efficiency (kcat/KM) and thermostability in the presence of salts
The activity of purified N5,N10-methenyltetrahydromethanopterin cyclohydrolase from Methanopyrus kandleri was found to increase up to 200-fold when potassium phosphate was added in high…
A novel function for the N-terminal nucleophile hydrolase fold demonstrated by the structure of an archaeal inosine monophosphate cyclohydrolase.
TLDR
Comparisons of the two types of IMP cyclohydrolase, PurO and PurH, revealed that there are no similarities in sequence, structure, or the active site architecture, suggesting that they are evolutionarily not related to each other.
A new use for a familiar fold: the X-ray crystal structure of GTP-bound GTP cyclohydrolase III from Methanocaldococcus jannaschii reveals a two metal ion catalytic mechanism.
TLDR
Three metal ions were located in the active site, two of which occupy positions that are analogous to those occupied by divalent metal ions in the structures of a number of palm domain containing proteins, such as DNA polymerase I.
Biosynthesis of pteridines. Reaction mechanism of GTP cyclohydrolase I.
[54] Synthesis and transformers of folic coenzymes II. Cyclohydrolase (5,10-methenyl to 10-formyl): 5,10-methenyltetrahydrofolic acid + H2O → 10-formyltetrahydrofolic acid
...
...