1.5.5.2: proline dehydrogenase

This is an abbreviated version!
For detailed information about proline dehydrogenase, go to the full flat file.

Reaction

Synonyms

bifunctional dye-linked L-proline/NADH dehydrogenase complex, dye-linked L-proline dehydrogenase, EC 1.5.99.8, FAD-dependent L-proline oxidoreductase, JcProDH, L-proline dehydrogenase, L-proline:FAD oxidoreductase, PdhB, PDHbeta, PF1246, PF1798, PH1364, PH1751, PRODH, proDH-B1, proDH-B2, PRODH/POX, ProDH1, proline dehydrogenase, proline dehydrogenase 1, proline dehydrogenase/oxidase, proline oxidase, proline/P5C dehydrogenase, prub, PutA, PutA flavoprotein, PutA proline dehydrogenase, Tc00.1047053506411.30, TcPRODH, TK0117, TK0122, TPpdhbeta, TtProDH

ECTree

     1 Oxidoreductases

         1.5 Acting on the CH-NH group of donors

             1.5.5 With a quinone or similar compound as acceptor

                1.5.5.2 proline dehydrogenase

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Results	in table
28048	AA Sequence
2	Application
1	CAS Registry Number
17	Cloned(Commentary)
28	Cofactor
7	Crystallization (Commentary)
181	Disease/ Diagnostics
9	Expression
35	General Information
1	General Stability
37	Inhibitors
26	kcat/KM [mM/s]
10	Ki Value [mM]
33	KM Value [mM]
11	Localization
1	Metals/Ions
19	Molecular Weight [Da]
14	Natural Substrates/ Products (Substrates)
52	Organism
12	Pathway
25	PDB ID
13	pH Optimum
1	pH Range
2	pH Stability
1	pI Value
19	Protein Variants
17	Purification (Commentary)
2	Reaction
3	Reaction Type
43	Reference
8	Source Tissue
9	Specific Activity [micromol/min/mg]
65	Substrates and Products (Substrate)
31	Subunits
92	Synonyms
1	Systematic Name
12	Temperature Optimum [°C]
1	Temperature Range [°C]
14	Temperature Stability [°C]
23	Turnover Number [1/s]

Engineering

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Engineering on EC 1.5.5.2 - proline dehydrogenase

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PROTEIN VARIANTS

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

D370A

Escherichia coli

-

mutant form of PutA86-601. The ratio of turnover-number to Km-value is 2.8fold lower than the ratio of the wild-type PutA86-601

658211

D370A/Y540F

Escherichia coli

-

mutant form of PutA86-601. The ratio of turnover-number to Km-value is 15fold lower than the ratio of the wild-type PutA86-601

658211

L432P

Escherichia coli

P09546

mutant form of PutA86-669, 5fold decrease in turnover-number and a severe loss in thermostability

658033

W194F

Escherichia coli

-

mutation in truncated enzyme containing residues 86-601, ratio of kcat to Km-value drops by 50%

671977

W194F/W211F

Escherichia coli

-

mutation in truncated enzyme containing residues 86-601, ratio of kcat to Km-value drops by 95%

671977

W211F

Escherichia coli

-

mutation in truncated enzyme containing residues 86-601, ratio of kcat to Km-value drops by 80%

671977

Y540A

Escherichia coli

P09546

a construct consisting of residue 86-630 of PutA is used

696361

Y540F

Escherichia coli

-

mutant form of PutA86-601. The ratio of turnover-number to Km-value is 5.8fold lower than the ratio of the wild-type PutA86-601

658211

Y540S

Escherichia coli

P09546

a construct consisting of residue 86-630 of PutA is used

696361

K110A

Mycobacterium tuberculosis

-

inactive

724389

Y203F

Mycobacterium tuberculosis

-

the mutant shows severely reduced catalytic efficiency compared to the wild type enzyme

724389

F10E/L12E

2 entries

additional information

8 entries

F10E/L12E

Thermus thermophilus

Q72IB8

construction of a variant with a more polar N-terminus, mutant F10E/L12E, because Thermus thermophilus ProDH (TtProDH), produced through fusion with maltose-binding protein (MBP) appears to be prone to aggregation. Preparation of TtProDH mutant variant DELTAABC, which lacks helices alphaA, alphaB and alphaC, the mutant shows no electron density for an AMP moiety of the cofactor

743834

F10E/L12E

Thermus thermophilus HB27 / ATCC BAA-163 / DSM 7039

-

construction of a variant with a more polar N-terminus, mutant F10E/L12E, because Thermus thermophilus ProDH (TtProDH), produced through fusion with maltose-binding protein (MBP) appears to be prone to aggregation. Preparation of TtProDH mutant variant DELTAABC, which lacks helices alphaA, alphaB and alphaC, the mutant shows no electron density for an AMP moiety of the cofactor

-

additional information

Arabidopsis thaliana

P92983

generation of an enzyme-deficient prodh1 mutant

741858

additional information

Arabidopsis thaliana

-

generation of an enzyme-deficient prodh1 mutant

741858

additional information

Escherichia coli

-

truncated enzyme containing residues 86-601 and only four Trp residues. Substantial conformational changes of truncated protein upon addition of proline

671977

additional information

Homo sapiens

O43272

expression of PRODH/POX in DLD-1 colorectal cancer cells significantly decreases basal and maximal respiration at both 3 and 5 days, and proline addition exacerbates this effect. PRODH/POX-dependent inhibition of respiration can be modulated by the duration of PRODH/POX expression and the availability of proline

741588

additional information

Pseudomonas putida

I2D0K8

the truncated form of Pseudomonas putida PutA shows proline dehydrogenase activity

742641

additional information

Pseudomonas putida

-

the truncated form of Pseudomonas putida PutA shows proline dehydrogenase activity

742641

additional information

Pseudomonas putida POS-F84

-

the truncated form of Pseudomonas putida PutA shows proline dehydrogenase activity

-

additional information

Vigna radiata

-

mutants deficient in proline dehydrogenase activity

392572