3.5.2.B3: (-)-gamma-lactamase

This is an abbreviated version!
For detailed information about (-)-gamma-lactamase, go to the full flat file.

Reaction

Synonyms

(-)-gamma-lactamase, mHG, MhIHL, SvGL

ECTree

3 Hydrolases

3.5 Acting on carbon-nitrogen bonds, other than peptide bonds

3.5.2 In cyclic amides

3.5.2.B3 (-)-gamma-lactamase

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Results	in table
2	Activating Compound
4	AA Sequence
4	Application
5	Cloned(Commentary)
3	Crystallization (Commentary)
7	General Information
1	kcat/KM [mM/s]
3	KM Value [mM]
4	Molecular Weight [Da]
4	Natural Substrates/ Products (Substrates)
11	Organism
5	pH Optimum
1	pH Range
1	pI Value
27	Protein Variants
2	Purification (Commentary)
2	Reaction
9	Reference
1	Specific Activity [micromol/min/mg]
19	Substrates and Products (Substrate)
1	Subunits
9	Synonyms
1	Systematic Name
5	Temperature Optimum [°C]
2	Temperature Range [°C]
3	Temperature Stability [°C]
2	Turnover Number [1/s]

Crystallization

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Crystallization on EC 3.5.2.B3 - (-)-gamma-lactamase

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purified apo-form, (+)-gamma-lactam bound, and (-)-gamma-lactam bound forms of the enzyme, X-ray diffraction structure determination and analysis, X-ray diffraction structure determination and analysis at 1.79-2.05 A resolution

Microbacterium hydrocarbonoxydans

E3SVS0

755471

the catalytic triad of the (-)-gamma-lactamase is comprised of residues Ser98, Asp230, and His259 and an oxyanion hole is formed by Tyr32 and Met99 according to the alignment results

Microbacterium hydrocarbonoxydans

E3SVS0

735828

to 1.73 A resolution, cubic space group F23 with unit cell parameters a=b=c=240.6 A. The trimeric enzyme has an alpha/beta hydrolase fold and closely resembles the cofactor free haloperoxidases

uncultured Microbacterium sp.

Q8GJP7

736630