Values CatLog read from this paper
Acetyltransfer precedes uridylyltransfer in the formation of UDP-N-acetylglucosamine in separable active sites of the bifunctional GlmU protein of Escherichia coli
PMID 8555230doi:10.1021/bi952275aOpen in Browse
The paper itself is not on this site: read it at the publisher. This page lists only the values CatLog read from it.
CatLog read 15 records (41 values) from this paper: GlmU (bifunctional acetyltransferase/uridylyltransferase) from Escherichia coli.
Read from the paper by an AI model and checked against the paper by a second, separate AI run; code converted the units. Values are in CatLog's units; each record opens in Browse with the line the paper prints and the checks.
| Enzyme | Organism | Substrate | kcat (s⁻¹) | Km (mM) | kcat/Km (mM⁻¹ s⁻¹) | Conditions | Open record |
|---|---|---|---|---|---|---|---|
| GlmU (bifunctional acetyltransferase/uridylyltransferase) | Escherichia coli | acetyl-coenzyme A | 55 | 0.32 | 170 | pH 7.6 | Open record: GlmU (bifunctional acetyltransferase/uridylyltransferase), acetyl-coenzyme A |
| GlmU (bifunctional acetyltransferase/uridylyltransferase) | Escherichia coli | butyryl-coenzyme A | 0.008 | — | — | pH 7.6 | Open record: GlmU (bifunctional acetyltransferase/uridylyltransferase), butyryl-coenzyme A |
| GlmU (bifunctional acetyltransferase/uridylyltransferase) | Escherichia coli | galactosamine 1-phosphate | 11 | 15 | 0.7 | pH 7.6 | Open record: GlmU (bifunctional acetyltransferase/uridylyltransferase), galactosamine 1-phosphate |
| GlmU (bifunctional acetyltransferase/uridylyltransferase) | Escherichia coli | glucosamine | 5 × 10⁻⁴ | — | — | pH 7.6 | Open record: GlmU (bifunctional acetyltransferase/uridylyltransferase), glucosamine |
| GlmU (bifunctional acetyltransferase/uridylyltransferase) | Escherichia coli | glucosamine 1-phosphate | 77 | 0.25 | 310 | pH 7.6 | Open record: GlmU (bifunctional acetyltransferase/uridylyltransferase), glucosamine 1-phosphate |
| GlmU (bifunctional acetyltransferase/uridylyltransferase) | Escherichia coli | glucose 1-phosphate | 0.2 | 2 | 0.1 | pH 7.6 | Open record: GlmU (bifunctional acetyltransferase/uridylyltransferase), glucose 1-phosphate |
| GlmU (bifunctional acetyltransferase/uridylyltransferase) | Escherichia coli | N-acetylgalactosamine 1-phosphate | 0.1 | 3.7 | 0.03 | pH 7.6 | Open record: GlmU (bifunctional acetyltransferase/uridylyltransferase), N-acetylgalactosamine 1-phosphate |
| GlmU (bifunctional acetyltransferase/uridylyltransferase) | Escherichia coli | N-acetylglucosamine 1-phosphate | 21 | 0.018 | 1.2 × 10³ | pH 7.6 | Open record: GlmU (bifunctional acetyltransferase/uridylyltransferase), N-acetylglucosamine 1-phosphate |
| GlmU (bifunctional acetyltransferase/uridylyltransferase) | Escherichia coli | propionyl-coenzyme A | 9.5 | 0.84 | 11 | pH 7.6 | Open record: GlmU (bifunctional acetyltransferase/uridylyltransferase), propionyl-coenzyme A |
| GlmU (bifunctional acetyltransferase/uridylyltransferase) | Escherichia coli | UDP-glucosamine | 33 | 1.3 | 25 | pH 7.6 | Open record: GlmU (bifunctional acetyltransferase/uridylyltransferase), UDP-glucosamine |
| GlmU (bifunctional acetyltransferase/uridylyltransferase) | Escherichia coli | uridine 5'-triphosphate | 24 | 0.017 | 1.4 × 10³ | pH 7.6 | Open record: GlmU (bifunctional acetyltransferase/uridylyltransferase), uridine 5'-triphosphate |
| GlmU (bifunctional acetyltransferase/uridylyltransferase)N-terminal proteolytic fragment M1-R331 | Escherichia coli | N-acetylglucosamine 1-phosphate | 1.2 | 0.01 | 120 | pH 7.6 | Open record: GlmU (bifunctional acetyltransferase/uridylyltransferase) N-terminal proteolytic fragment M1-R331, N-acetylglucosamine 1-phosphate |
| GlmU (bifunctional acetyltransferase/uridylyltransferase)N-terminal proteolytic fragment M1-R331 | Escherichia coli | uridine 5'-triphosphate | 1.2 | 0.012 | 100 | pH 7.6 | Open record: GlmU (bifunctional acetyltransferase/uridylyltransferase) N-terminal proteolytic fragment M1-R331, uridine 5'-triphosphate |
| GlmU (bifunctional acetyltransferase/uridylyltransferase)variant GST-M180-K456 | Escherichia coli | acetyl-coenzyme A | 0.4 | 1.1 | 0.4 | pH 7.6 | Open record: GlmU (bifunctional acetyltransferase/uridylyltransferase) variant GST-M180-K456, acetyl-coenzyme A |
| GlmU (bifunctional acetyltransferase/uridylyltransferase)variant GST-M180-K456 | Escherichia coli | glucosamine 1-phosphate | 0.5 | 0.37 | 1 | pH 7.6 | Open record: GlmU (bifunctional acetyltransferase/uridylyltransferase) variant GST-M180-K456, glucosamine 1-phosphate |