3.4.23.51: HycI peptidase

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For detailed information about HycI peptidase, go to the full flat file.

Reaction

This enzyme specifically removes a 32-amino acid peptide from the C-terminus of the precursor of the large subunit of hydrogenase 3 in Escherichia coli by cleavage at the C-terminal side of Arg537. =

Synonyms

HycE processing protein, HYCI, HycI endopeptidase

ECTree

3 Hydrolases

3.4 Acting on peptide bonds (peptidases)

3.4.23 Aspartic endopeptidases

3.4.23.51 HycI peptidase

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Results	in table
1050	AA Sequence
2	Cloned(Commentary)
2	Crystallization (Commentary)
1	Inhibitors
3	Metals/Ions
3	Molecular Weight [Da]
5	Natural Substrates/ Products (Substrates)
8	Organism
1	Pathway
1	pI Value
4	Protein Variants
4	Purification (Commentary)
1	Reaction
8	Reference
12	Substrates and Products (Substrate)
2	Subunits
7	Synonyms

Crystallization

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Crystallization on EC 3.4.23.51 - HycI peptidase

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solution structure of Escherichia coli HycI determined by high resolution nuclear magnetic resonance spectroscopy. The overall structure is similar to the crystal structure of holo-HybD in the same family. HycI shows an open conformation at the putative nickel-binding site, whereas HybD adopts a closed conformation

Escherichia coli

P0AEV9

680866

sitting drop vapor diffusion method, using 28% (w/v) polyethylene glycol 400, 0.2 M CaCl2, and 0.1 M Na-HEPES (pH 7.5), at 20°C

Escherichia coli K-12

P0AEV9

711075